A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
A phenothiazine with actions similar to CHLORPROMAZINE. It is used as an antipsychotic and an antiemetic.
Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.
A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
A group of compounds that contain the structure SO2NH2.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The rate dynamics in chemical or physical systems.
A chelating agent relatively more specific for calcium and less toxic than EDETIC ACID.
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
Nucleoside-2',3'-cyclic phosphate nucleotidohydrolase. Enzymes that catalyze the hydrolysis of the 2'- or 3'- phosphate bonds of 2',3'-cyclic nucleotides. Also hydrolyzes nucleoside monophosphates. Includes EC 3.1.4.16 and EC 3.1.4.37. EC 3.1.4.-.
The prototypical phenothiazine antipsychotic drug. Like the other drugs in this class chlorpromazine's antipsychotic actions are thought to be due to long-term adaptation by the brain to blocking DOPAMINE RECEPTORS. Chlorpromazine has several other actions and therapeutic uses, including as an antiemetic and in the treatment of intractable hiccup.
Cation-transporting proteins that utilize the energy of ATP hydrolysis for the transport of CALCIUM. They differ from CALCIUM CHANNELS which allow calcium to pass through a membrane without the use of energy.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Enzymes that catalyze the hydrolysis of CYCLIC AMP to form adenosine 5'-phosphate. The enzymes are widely distributed in animal tissue and control the level of intracellular cyclic AMP. Many specific enzymes classified under this heading demonstrate additional spcificity for 3',5'-cyclic IMP and CYCLIC GMP.
A BRAIN-specific substrate for PROTEIN KINASE C that binds CALMODULIN and is involved in regulation of CALCIUM SIGNALING.
Terpenes of five units of HEMITERPENES, formed from geranylfarnesyl pyrophosphate.
Basic polypeptide from the venom of the honey bee (Apis mellifera). It contains 26 amino acids, has cytolytic properties, causes contracture of muscle, releases histamine, and disrupts surface tension, probably due to lysis of cell and mitochondrial membranes.
A CALCIUM and CALMODULIN-dependent cyclic nucleotide phosphodiesterase subfamily. The three members of this family are referred to as type 1A, type 1B, and type 1C and are each product of a distinct gene. In addition, multiple enzyme variants of each subtype can be produced due to multiple alternative mRNA splicing. Although the type 1 enzymes are classified as 3',5'-cyclic-AMP phosphodiesterases (EC 3.1.4.17), some members of this class have additional specificity for CYCLIC GMP.
A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.
A monomeric calcium-calmodulin-dependent protein kinase subtype that is expressed in a broad variety of mammalian cell types. Its expression is regulated by the action of CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE. Several isoforms of this enzyme subtype are encoded by distinct genes.
Compounds containing dibenzo-1,4-thiazine. Some of them are neuroactive.
A genus of ciliate protozoa that is often large enough to be seen by the naked eye. Paramecia are commonly used in genetic, cytological, and other research.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Calcium-binding motifs composed of two helices (E and F) joined by a loop. Calcium is bound by the loop region. These motifs are found in many proteins that are regulated by calcium.
A drug formerly used in the treatment of angina pectoris but superseded by less hazardous drugs. Prenylamine depletes myocardial catecholamine stores and has some calcium channel blocking activity. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1406)
Venoms produced by the wasp (Vespid) family of stinging insects, including hornets; the venoms contain enzymes, biogenic amines, histamine releasing factors, kinins, toxic polypeptides, etc., and are similar to bee venoms.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
An enzyme that catalyzes the conversion of ATP and PHOSPHORYLASE B to ADP and PHOSPHORYLASE A.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
Signal transduction mechanisms whereby calcium mobilization (from outside the cell or from intracellular storage pools) to the cytoplasm is triggered by external stimuli. Calcium signals are often seen to propagate as waves, oscillations, spikes, sparks, or puffs. The calcium acts as an intracellular messenger by activating calcium-responsive proteins.
A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.
One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Measurement of the intensity and quality of fluorescence.
Toluenes in which one hydrogen of the methyl group is substituted by an amino group. Permitted are any substituents on the benzene ring or the amino group.
A phenothiazine used in the treatment of PSYCHOSES. Its properties and uses are generally similar to those of CHLORPROMAZINE.
The sum of the weight of all the atoms in a molecule.
One of the three polypeptide chains that make up the TROPONIN complex of skeletal muscle. It is a calcium-binding protein.
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Proteins prepared by recombinant DNA technology.
A subclass of myosins found generally associated with actin-rich membrane structures such as filopodia. Members of the myosin type I family are ubiquitously expressed in eukaryotes. The heavy chains of myosin type I lack coiled-coil forming sequences in their tails and therefore do not dimerize.
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Venoms obtained from Apis mellifera (honey bee) and related species. They contain various enzymes, polypeptide toxins, and other substances, some of which are allergenic or immunogenic or both. These venoms were formerly used in rheumatism to stimulate the pituitary-adrenal system.
The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

AMP-activated protein kinase phosphorylation of endothelial NO synthase. (1/4572)

The AMP-activated protein kinase (AMPK) in rat skeletal and cardiac muscle is activated by vigorous exercise and ischaemic stress. Under these conditions AMPK phosphorylates and inhibits acetyl-coenzyme A carboxylase causing increased oxidation of fatty acids. Here we show that AMPK co-immunoprecipitates with cardiac endothelial NO synthase (eNOS) and phosphorylates Ser-1177 in the presence of Ca2+-calmodulin (CaM) to activate eNOS both in vitro and during ischaemia in rat hearts. In the absence of Ca2+-calmodulin, AMPK also phosphorylates eNOS at Thr-495 in the CaM-binding sequence, resulting in inhibition of eNOS activity but Thr-495 phosphorylation is unchanged during ischaemia. Phosphorylation of eNOS by the AMPK in endothelial cells and myocytes provides a further regulatory link between metabolic stress and cardiovascular function.  (+info)

Calmodulin mediates calcium-dependent activation of the intermediate conductance KCa channel, IKCa1. (2/4572)

Small and intermediate conductance Ca2+-activated K+ channels play a crucial role in hyperpolarizing the membrane potential of excitable and nonexcitable cells. These channels are exquisitely sensitive to cytoplasmic Ca2+, yet their protein-coding regions do not contain consensus Ca2+-binding motifs. We investigated the involvement of an accessory protein in the Ca2+-dependent gating of hIKCa1, a human intermediate conductance channel expressed in peripheral tissues. Cal- modulin was found to interact strongly with the cytoplasmic carboxyl (C)-tail of hIKCa1 in a yeast two-hybrid system. Deletion analyses defined a requirement for the first 62 amino acids of the C-tail, and the binding of calmodulin to this region did not require Ca2+. The C-tail of hSKCa3, a human neuronal small conductance channel, also bound calmodulin, whereas that of a voltage-gated K+ channel, mKv1.3, did not. Calmodulin co-precipitated with the channel in cell lines transfected with hIKCa1, but not with mKv1. 3-transfected lines. A mutant calmodulin, defective in Ca2+ sensing but retaining binding to the channel, dramatically reduced current amplitudes when co-expressed with hIKCa1 in mammalian cells. Co-expression with varying amounts of wild-type and mutant calmodulin resulted in a dominant-negative suppression of current, consistent with four calmodulin molecules being associated with the channel. Taken together, our results suggest that Ca2+-calmodulin-induced conformational changes in all four subunits are necessary for the channel to open.  (+info)

Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites. (3/4572)

NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase family protein, is known to bind to C-terminal ends of N-methyl-D-aspartate receptor 2B (NR2B) through its PDZ (PSD-95/Dlg/ZO-1) domains. NE-dlg/SAP102 and NR2B colocalize at synaptic sites in cultured rat hippocampal neurons, and their expressions increase in parallel with the onset of synaptogenesis. We have identified that NE-dlg/SAP102 interacts with calmodulin in a Ca2+-dependent manner. The binding site for calmodulin has been determined to lie at the putative basic alpha-helix region located around the src homology 3 (SH3) domain of NE-dlg/SAP102. Using a surface plasmon resonance measurement system, we detected specific binding of recombinant NE-dlg/SAP102 to the immobilized calmodulin with a Kd value of 44 nM. However, the binding of Ca2+/calmodulin to NE-dlg/SAP102 did not modulate the interaction between PDZ domains of NE-dlg/SAP102 and the C-terminal end of rat NR2B. We have also identified that the region near the calmodulin binding site of NE-dlg/SAP102 interacts with the GUK-like domain of PSD-95/SAP90 by two-hybrid screening. Pull down assay revealed that NE-dlg/SAP102 can interact with PSD-95/SAP90 in the presence of both Ca2+ and calmodulin. These findings suggest that the Ca2+/calmodulin modulates interaction of neuronal membrane-associated guanylate kinase proteins and regulates clustering of neurotransmitter receptors at central synapses.  (+info)

Properties of filament-bound myosin light chain kinase. (4/4572)

Myosin light chain kinase binds to actin-containing filaments from cells with a greater affinity than to F-actin. However, it is not known if this binding in cells is regulated by Ca2+/calmodulin as it is with F-actin. Therefore, the binding properties of the kinase to stress fibers were examined in smooth muscle-derived A7r5 cells. Full-length myosin light chain kinase or a truncation mutant lacking residues 2-142 was expressed as chimeras containing green fluorescent protein at the C terminus. In intact cells, the full-length kinase bound to stress fibers, whereas the truncated kinase showed diffuse fluorescence in the cytoplasm. After permeabilization with saponin, the fluorescence from the truncated kinase disappeared, whereas the fluorescence of the full-length kinase was retained on stress fibers. Measurements of fluorescence intensities and fluorescence recovery after photobleaching of the full-length myosin light chain kinase in saponin-permeable cells showed that Ca2+/calmodulin did not dissociate the kinase from these filaments. However, the filament-bound kinase was sufficient for Ca2+-dependent phosphorylation of myosin regulatory light chain and contraction of stress fibers. Thus, dissociation of myosin light chain kinase from actin-containing thin filaments is not necessary for phosphorylation of myosin light chain in thick filaments. We note that the distance between the N terminus and the catalytic core of the kinase is sufficient to span the distance between thin and thick filaments.  (+info)

cAMP inhibits translation by inducing Ca2+/calmodulin-independent elongation factor 2 kinase activity in IPC-81 cells. (5/4572)

Treatment of IPC-81 cells led to inhibition of protein synthesis, which was accompanied by an increase in the average size of polysomes and a decreased rate of elongation, indicating that it involved inhibition of peptide chain elongation. This inhibition was also associated with increased phosphorylation of elongation factor eEF2 (which inhibits its activity) and enhanced Ca2+/calmodulin-independent activity of eEF2 kinase. Previous work has shown that phosphorylation of eEF2 kinase by cAMP-dependent protein kinase (cAPK) in vitro induces such activator-independent activity, and the present data show that such a mechanism can occur in intact cells to link physiological levels of cAPK activation with inhibition of protein synthesis.  (+info)

T-cell stimulation through the T-cell receptor/CD3 complex regulates CD2 lateral mobility by a calcium/calmodulin-dependent mechanism. (6/4572)

T lymphocyte activation through the T cell receptor (TCR)/CD3 complex alters the avidity of the cell surface adhesion receptor CD2 for its ligand CD58. Based on the observations that activation-associated increases in intracellular [Ca2+] ([Ca2+]i) strengthen interactions between T cells and antigen-presenting cells, and that the lateral mobility of cell surface adhesion receptors is an important regulator of cellular adhesion strength, we postulated that [Ca2+]i controls CD2 lateral mobility at the T cell surface. Human Jurkat T leukemia cells were stimulated by antibody-mediated cross-linking of the TCR/CD3 complex. CD2 was labeled with a fluorescently conjugated monoclonal antibody. Quantitative fluorescence microscopy techniques were used to measure [Ca2+]i and CD2 lateral mobility. Cross-linking of the TCR/CD3 complex caused an immediate increase in [Ca2+]i and, 10-20 min later, a decrease in the fractional mobility of CD2 from the control value of 68 +/- 1% to 45 +/- 2% (mean +/- SEM). One to two hours after cell stimulation the fractional mobility spontaneously returned to the control level. Under these and other treatment conditions, the fraction of cells with significantly elevated [Ca2+]i was highly correlated with the fraction of cells manifesting significantly reduced CD2 mobility. Pretreatment of cells with a calmodulin inhibitor or a calmodulin-dependent kinase inhibitor prevented Ca2+-mediated CD2 immobilization, and pretreatment of cells with a calcineurin phosphatase inhibitor prevented the spontaneous reversal of CD2 immobilization. These data suggest that T cell activation through the TCR/CD3 complex controls CD2 lateral mobility by a Ca2+/calmodulin-dependent mechanism, and that this mechanism may involve regulated phosphorylation and dephosphorylation of CD2 or a closely associated protein.  (+info)

Suramin and suramin analogs activate skeletal muscle ryanodine receptor via a calmodulin binding site. (7/4572)

Contraction of skeletal muscle is triggered by the rapid release of Ca2+ from the sarcoplasmic reticulum via the ryanodine receptor/calcium-release channel. The trypanocidal drug suramin is an efficient activator of the ryanodine receptor. Here, we used high-affinity [3H]ryanodine binding to sarcoplasmic reticulum from rabbit skeletal muscle to screen for more potent analogs of suramin. This approach resulted in the identification of NF307, which accelerates the association rate of [3H]ryanodine binding with an EC50 = 91 +/- 7 microM at 0.19 microM calculated free Ca2+. In single-channel recordings with the purified ryanodine receptor, NF307 increased mean open probability at 0.6 microM Ca2+ from 0.020 +/- 0.006 to 0.53 +/- 0.07 with no effect on current amplitude and unitary conductance. Like caffeine, NF307 exerts a very pronounced Ca2+-sensitizing effect (EC50 of Ca2+ shifted approximately 10-fold by saturating NF307 concentrations). Conversely, increasing concentrations of free Ca2+ sensitized the receptor for NF307 (EC50 = 14.6 +/- 3.5 microM at 0.82 microM estimated free Ca2+). The effects of NF307 and caffeine on [3H]ryanodine binding were additive, irrespective of the Ca2+ concentration. In contrast, the effects of calmodulin, which activates and inhibits the ryanodine receptor in the absence and presence of Ca2+, respectively, and of NF307 were mutually antagonistic. If the purified ryanodine receptor was prebound to a calmodulin-Sepharose matrix, 100 microM NF307 and 300 microM suramin eluted the purified ryanodine receptor to an extent that was comparable to the effect of 10 microM calmodulin. We conclude that NF307 and suramin interact directly with a calmodulin binding domain of the ryanodine receptor. Because of its potent calcium-sensitizing effect, NF307 may represent a lead compound in the search of synthetic ryanodine receptor ligands.  (+info)

Dynamic and quantitative Ca2+ measurements using improved cameleons. (8/4572)

Cameleons are genetically-encoded fluorescent indicators for Ca2+ based on green fluorescent protein variants and calmodulin (CaM). Because cameleons can be targeted genetically and imaged by one- or two-photon excitation microscopy, they offer great promise for monitoring Ca2+ in whole organisms, tissues, organelles, and submicroscopic environments in which measurements were previously impossible. However, the original cameleons suffered from significant pH interference, and their Ca2+-buffering and cross-reactivity with endogenous CaM signaling pathways was uncharacterized. We have now greatly reduced the pH-sensitivity of the cameleons by introducing mutations V68L and Q69K into the acceptor yellow green fluorescent protein. The resulting new cameleons permit Ca2+ measurements despite significant cytosolic acidification. When Ca2+ is elevated, the CaM and CaM-binding peptide fused together in a cameleon predominantly interact with each other rather than with free CaM and CaM-dependent enzymes. Therefore, if cameleons are overexpressed, the primary effect is likely to be the unavoidable increase in Ca2+ buffering rather than specific perturbation of CaM-dependent signaling.  (+info)

TY - JOUR. T1 - Fluorescence analysis of calmodulin mutants containing tryptophan. T2 - Conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II. AU - Prendergast, Franklyn G.. PY - 1991. Y1 - 1991. N2 - Peptide-induced conformational changes in five isofunctional mutants of calmodulin (CaM), each bearing a single tryptophan residue either at the seventh position of each of the four calcium-binding loops (i.e., amino acids 26, 62, 99, and 135) or in the central helix (amino acid 81) were studied by using fluorescence spectroscopy. The peptides RS20F and RS20CK correspond to CaM-binding amino acid sequence segments of either nonmuscle myosin light chain kinase (nmMLCK) or calmodulin-dependent protein kinase II (CaMPK-II), respectively. Both steady-state and time-resolved fluorescence data were collected from the various peptide-CaM complexes. Steady-state fluorescence intensity measurements indicated that, in the presence of an excess of ...
Multiple calmodulin (CaM) isoforms are expressed in plants, but their biochemical characteristics are not well resolved. Here we show the differential regulation exhibited by two soya bean CaM isoforms (SCaM-1 and SCaM-4) for the activation of five CaM-dependent enzymes, and the Ca2+ dependence of their target enzyme activation. SCaM-1 activated myosin light-chain kinase as effectively as brain CaM (Kact 1.8 and 1.7nM respectively), but SCaM-4 produced no activation of this enzyme. Both CaM isoforms supported near maximal activation of CaM-dependent protein kinase II (CaM KII), but SCaM-4 exhibited approx.12-fold higher Kact than SCaM-1 for CaM KII phosphorylation of caldesmon. The SCaM isoforms showed differential activation of plant and animal Ca2+-ATPases. The plant Ca2+-ATPase was activated maximally by both isoforms, while the erythrocyte Ca2+-ATPase was activated only by SCaM-1. Plant glutamate decarboxylase was activated fully by SCaM-1, but SCaM-4 exhibited an approx. 4-fold increase ...
Techniques such as X-ray structural analysis offer snapshots, at best, of steps in this intracellular work flow. But single-molecule atomic-force spectroscopy has opened a new window on such dynamic processes.. Professor Matthias Rief and colleagues at the Technische Universitaet Muenchen had previously shown that they could fix a single calmodulin molecule between a surface and the cantilever tip of a specially built atomic-force microscope, expose it to calcium ions in solution, induce peptide binding and unbinding, and measure changes in the molecules mechanical properties as it did its work. What is special about our technique, Rief says, is that we can work directly in aqueous solution. We can make our measurements in exactly the conditions under which the protein works in its natural environment. So we can directly observe how the calmodulin snatches the amino acid chain and folds itself, to hold its target fast. Measuring the force needed to bend the calmodulin molecule out of its ...
Elsewhere, we have reported the structure of a rat calmodulin gene and two distinct rat calmodulin cDNAs, pRCM1 and pRCM3. Here, I report the cloning and sequencing of the third calmodulin cDNA (pRCM4) and two additional rat calmodulin genes. The original calmodulin gene is named CaM I (pRCM1) and t …
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N-methyl-D-aspartate (NMDA) receptors are calcium-permeable ion channels assembled from four subunits that each have a common membrane topology. The intracellular carboxyl terminal domain (CTD) of each subunit varies in length, is least conserved between subunits, and binds multiple intracellular proteins. We defined a region of interest in the GluN2A CTD, downstream of well-characterized membraneproximal motifs, that shares only 29% sequence similarity with the equivalent region of GluN2B. GluN2A (amino acids 875-1029) was fused to GST and used as a bait to identify proteins from mouse brain with the potential to bind GluN2A as a function of calcium. Using mass spectrometry we identified calmodulin as a calcium-dependent GluN2A binding partner. Equilibrium fluorescence spectroscopy experiments indicate that Ca²⁺/calmodulin binds GluN2A with high affinity (5.2 ± 2.4 nM) in vitro. Direct interaction of Ca²⁺/calmodulin with GluN2A was not affected by disruption of classic sequence motifs ...
Involvement of calmodulin and calmodulin-like proteins in plant responses to abiotic stresses Published In Frontiers in Plant Science, 6:600, 2015, by Houqing Zeng, Luqin Xu, Amarjeet Singh, Huizhong Wang, Liqun Du, B. W. Poovaiah ...
TY - JOUR. T1 - Calmodulin binds to the C terminus of sodium channels Nav1.4 and Navl.6 and differentially modulates their functional properties. AU - Herzog, Raimund I.. AU - Liu, Chuanju. AU - Waxman, Stephen G.. AU - Cummins, Theodore R.. PY - 2003/9/10. Y1 - 2003/9/10. N2 - Modulation of voltage-gated sodium channels (VGSC) can have a major impact on cell excitability. Analysis of calmodulin (CaM) binding to GST-fusion proteins containing the C-terminal domains of Navl.l-Na vl.9 indicates that some of the tetrodotoxin-sensitive VGSC isoforms, including Navl.4 and Navl.6, are able to bind CaM in a calcium-independent manner. Here we demonstrate that association with CaM is important for functional expression of Nav1.4 and Navl.6 VGSCs. Disrupting the interaction between CaM and the C terminus of Na vl.4 and Navl.6 channels reduced current amplitude by 99 and 62%, respectively. Overexpression of CaM increased the current generated by Navl.4 and Navl.6 C-terminal mutant constructs that ...
The calcium-signaling network is an important transducer of internal and external stimuli in plants. These signals are transduced by a divers set of calcium-sensors such as calmodulin and calmodulin like proteins. In this work, AFG1L2 (AFG1 like protein 2) was characterized as a calmodulin binding protein that belongs to the family of AAA+ proteins (ATPases associated with various cellular activities). Using GFP fusion constructs it was possible to determine the in vivo localization of AFG1L2 in mitochondria and also to confirm the dual localization of a previously described homologe, AFG1L1, to mitochondria and chloroplasts. The interaction between AFG1L2 and calmodulin is calcium dependent and the calmodulin binding site of the AFG1L2 protein is in the AAA domain at a site homologous to the AFG1L1 protein, in very close proximity to the Walker A Motif, which is essential for ATP hydrolysis. It could be shown that ATP and ADP intensify the interaction between AFG1L2 and calmodulin. AAA-proteins ...
Mutations: The following mutations were used: Camn339, recessive RNA null mutation (Heimanet al. 1996); Cam7, recessive ethyl methanesulfonate mutation (Nelsonet al. 1997); Cam352, recessive hypomorph, generated by excision of a P element in 5′ flanking DNA (Scottet al. 1997); Cam3909, recessive hypomorph generated by a P insertion 60 bp 5′ of the transcription start site (Harvieet al. 1998); Ryr16, recessive mutation of the ryanodine receptor gene (Ryr; Sullivanet al. 2000); Df(2R)H3E1, deficiency with breakpoints at 44D1-4 and 44F12 (Bloomington Stock Center); Ca-α1DX7, embryonic lethal Ca-α1D mutation (Eberlet al. 1998); Ca-α1DAR66, hypomorphic Ca-α1D mutation (Eberlet al. 1998; Renet al. 1998); and cn1, cinnabar (Bloomington Stock Center).. Gal4 lines: We used the following Gal4 lines: 24B-Gal4, P{GawB}how24B, an insertion into held out wings that expresses Gal4 in muscle (Brand and Perrimon 1993); elav-Gal4, Gal4 expressed under the elav promoter in neurons at all developmental ...
The regulation of the guinea-pig pancreatic acinar plasma membrane Ca2+ pump by protein kinase A, protein kinase C and calmodulin was investigated. The results were compared with the effects of these regulators on the high affinity Ca2+-ATPase found in this membrane preparation. The catalytic subunit of cyclic AMP-dependent protein kinase stimulated Ca2+ transport 2-fold, but had no effect on Ca2+-dependent ATPase activity. Purified protein kinase C, the phorbol ester 12-O-tetradecanoyl phorbol-13-acetate and diacylglycerol derivative, 1-stearoyl-2-arachidonoyl-sn-glycerol, failed to stimulate the Ca2+-uptake but augmented the Ca2+-dependent ATPase activity. Exogenously added calmodulin failed to stimulate either activity. In addition, two antagonists of calmodulin activity, trifluoperazine and compound 48/80 produced a concentration-dependent inhibition of Ca2+-transport. These data suggest the presence of endogenous calmodulin within guinea-pig pancreatic acinar plasma membranes. Both calmodulin
Biological systems primarily use proteins to sense and respond to other molecules. We sought to engineer a protein-based platform as the basis of a biologically emulative biosensor. This biosensor platform is especially powerful if both the analyte sensitivity and transduction method can be straightforwardly customized to respond to important targets. Here we show our attempts to demonstrate the modularity of a pre-existing protein biosensor through such customization. The calcium-binding protein calmodulin has already been engineered to exhibit enzymatic switching in response to peptide binding through fusion to a split TEM1 ß-lactamase. To extend this platform, we first evolved the calmodulin-ß-lactamase fusion (BlaCaM) to exhibit sensitivity to a previously inactive peptide, Staphylococcus aureus ∂-toxin, through random mutagenesis of the calmodulin portion of BlaCaM, followed by screening the purified library for ß-lactamase activity. Second, we altered the transduction domain by ...
Calmodulin (CaM) (an abbreviation for CALcium MODULated proteIN) is a calcium-binding protein expressed in all eukaryotic cells. It can bind to and regulate a number of different protein targets, thereby affecting many different cellular functions. Calmodulin 1 is one of nearly twenty human calmodulins.Calmodulinis the archetype of the family of calcium-modulated proteins of which nearly 20 members have been found. They are identified by their occurrence in the cytosol or on membranes facing the cytosol and by a high affinity for calcium. Calmodulin contains 148 amino acids and has 4 calcium-binding motifs. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters.
Transcription factor regulating the cell cycle specific transcription of a spindle pole body (SPB) calmodulin binding protein SPC110. Required for full induction of SPC110 transcription in late G1. Binds to DNA consensus sequence 5-[AT]AA[TC]AAACAA[AT]-3. Dosage dependent suppressor of calmodulin mutants which have specific defects in SPB assembly.
It is an open question how the multiple special and temporal scales involved in intracellular Ca2+ handling within the STDP models affect the plasticity outcomes predicted by these models. Hebbian or associative plasticity is triggered by postsynaptic Ca2+ influx which activates calmodulin and CaMKII. The influx of Ca2+ through voltage-dependent NMDA receptors and Ca2+ channels is regulated by Ca2+ -activated K+ channels (SK-channels) providing negative feedback regulation of postsynaptic [Ca2+]. Using 3-dimensional modelling of Ca2+ and calmodulin dynamics within dendritic spines we show that the non-linear relationship between Ca2+ influx and calmodulin activation endows SK-channels with the ability to gate calmodulin activation and therefore the induction of Hebbian synaptic plasticity. Since SK-channels are inhibited by several neuro-modulator receptors including acetylcholine and noradrenaline, the gating of synaptic plasticity by SK-channels could represent a common mechanism by which ...
It is an open question how the multiple special and temporal scales involved in intracellular Ca2+ handling within the STDP models affect the plasticity outcomes predicted by these models. Hebbian or associative plasticity is triggered by postsynaptic Ca2+ influx which activates calmodulin and CaMKII. The influx of Ca2+ through voltage-dependent NMDA receptors and Ca2+ channels is regulated by Ca2+ -activated K+ channels (SK-channels) providing negative feedback regulation of postsynaptic [Ca2+]. Using 3-dimensional modelling of Ca2+ and calmodulin dynamics within dendritic spines we show that the non-linear relationship between Ca2+ influx and calmodulin activation endows SK-channels with the ability to gate calmodulin activation and therefore the induction of Hebbian synaptic plasticity. Since SK-channels are inhibited by several neuro-modulator receptors including acetylcholine and noradrenaline, the gating of synaptic plasticity by SK-channels could represent a common mechanism by which ...
Background: Recent genetic studies identified mutations in CALM1 or CALM2, 2 of the 3 human genes encoding calmodulin (CaM), in both catecholaminergic polymorphic ventricular tachycardia (CPVT) and long QT syndrome (LQTS). CPVT is commonly caused by mutations in sarcoplasmic reticulum genes that increase diastolic Ca leakage through ryanodine receptor (RyR2) Ca relase channels, whereas LQTS is usually caused by dysfunctional plasma membrane ion channels. How mutant CaM causes either CPVT or LQTS is unknown.. Objective: To gain mechanistic insight into how CaM mutations cause divergent human arrhythmia phenotypes.. Methods and Results: We prepared recombinant wild-type (WT) and mutant CaM proteins associated with either CPVT (N54I, N98S) or LQTS ( F142L, D130G). LQTS CaM mutations drastically reduce Ca binding affinity to CaM, whereas CPVT mutations have either no effect (N54I) or slightly reduce Ca binding affinity (N98S). At physiological free CaM [100 nM] and Ca [120 nM], CPVT CaMs ...
In article ,95059.080316RJC8 at psuvm.psu.edu, Richard Cyr ,RJC8 at psuvm.psu.edu, writes: , Does anyone know of a reference wher , e the extinction coefficient of CaM was determined? The Merck index gives the extinction coefficient(1%) at A280 to be 2.1 Christine Dept. of Biochemistry hughe014 at mc.duke.edu ...
(1994) Means. FEBS Letters. Calcium and its ubiquitous intracellular receptor calmodulin are required for cell proliferation. Studies in a variety of model systems are beginning to identify components of the calcium/calmodulin cascade required for movement of quiescent cells into the cell cycle a...
The vacuolar calmodulin (CaM)-stimulated Ca2+-ATPase, BCA1p, in cauliflower (Brassica oleracea) has an extended N terminus, which was suggested to contain a CaM-binding domain (S. Malmstrom, P. Askerlund, M.G. Palmgren [1997] FEBS Lett 400: 324328). The goal of the present study was to determine the role of the N terminus in regulating BCA1p. Western analysis using three different antisera showed that the N terminus of BCA1p is cleaved off by trypsin and that the N terminus contains the CaM-binding domain. Furthermore, the expressed N terminus binds CaM in a Ca2+dependent manner. A synthetic peptide corresponding to the CaM-binding domain of BCA1p (Ala-19 to Leu-43) strongly inhibited ATP-dependent Ca2+ pumping by BCA1p in cauliflower low-density membranes, indicating that the CaM-binding region of BCA1p also has an autoinhibitory function. The expressed N terminus of BCA1p and a synthetic peptide (Ala-19 to Met-39) were good substrates for phosphorylation by protein kinase C. Sequencing of the ...
Structural and biophysical studies reveal how CaMKII kinases, which are important for cellular learning and memory, are switched on by binding of Ca2+/calmodulin.
Rabbit polyclonal Calmodulin (phospho T79 + S81) antibody validated for WB, ELISA, IHC, ICC/IF and tested in Human. Referenced in 2 publications. Immunogen…
Adunyah S.E.; Dean W.L., 1987: Regulation of human platelet membrane calcium transport by cyclic amp and calmodulin dependent phosphorylation
Ca2+-calmodulin binding to caldesmon and the caldesmon-actin-tropomyosin complex. Its role in Ca2+regulation of the activity of synthetic smooth-muscle thin filaments Academic Article ...
Many signalling pathways in plants are regulated by the second messenger calcium (Ca2+). In the standard model, Ca2+-sensor proteins, such as CaM (calmodulin), detect Ca2+ signals and subsequently regulate downstream targets to advance the signal transduction cascade. In addition to CaM, plants possess many CMLs (CaM-like proteins) that are predicted to function as Ca2+ sensors, but which remain largely uncharacterized. In the present study, we examined the biochemical properties, subcellular localization and tissue-specific distribution of Arabidopsis CML43. Our data indicate that CML43 displays characteristics typical of Ca2+ sensors, including high-affinity Ca2+ binding, conformational changes upon Ca2+ binding that expose hydrophobic regions and stabilization of structure in the presence of Mg2+ or Ca2+. In vivo localization analysis demonstrates that CML43 resides in cytosolic and nuclear compartments. Transgenic plants expressing a CML43:GUS (β-glucoronidase) promoter reporter gene ...
The limited ability of cytotoxic CD8+ T cells to infiltrate solid tumors and function within the tumor microenvironment presents a major roadblock to effective immunotherapy. Ion channels and Ca2+-dependent signaling events control the activity of T cells and are implicated in the failure of immune surveillance in cancer. Reduced KCa3.1 channel activity mediates the heightened inhibitory effect of adenosine on the chemotaxis of circulating T cells from head and neck squamous cell carcinoma (HNSCC) patients. Herein, we conducted experiments that elucidate the mechanisms of KCa3.1 dysfunction and impaired chemotaxis in HNSCC CD8+ T cells. The Ca2+ sensor calmodulin (CaM) controls multiple cellular functions including KCa3.1 activation. Our data showed that CaM expression is lower in HNSCC than healthy donor (HD) T cells. This reduction was due to an intrinsic decrease in the genes encoding CaM combined to the failure of HNSCC T cells to upregulate CaM upon activation. Furthermore, the reduction in CaM was
The RbcS genes encode the small subunits of rubisco; the expression of these genes is controlled in a light-dependent and independent manner. It has been reported that intracellular calmodulin (CaM) is involved in light-dependent RbcS expression. In this report, the role of extracellular CaM in regulating expression of RbcS in darkness was examined. The time course of expression of RbcS-GUS and that of the secretion of CaM in the suspended transgenic tobacco cells in darkness were very similar. Both showed initial increase followed by decline with maximum CaM secretion preceding maximum GUS expression by 24 h. The concentration of CaM in the culture medium is regulated light independently. Purified CaM alone added to the media enhanced RbcS-GUS expression in darkness. The addition of membrane-impermeable CaM inhibitors, such as anti-CaM antiserum or W7-agarose, repressed the expression of RbcS-GUS in darkness, but this inhibitory effect was completely reversed by adding exogenous purified CaM. ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the l …
Forkhead Transcription Factor; Drives S-phase Specific Expression Of Genes Involved In Chromosome Segregation, Spindle Dynamics, And Budding; Suppressor Of Calmodulin Mutants With Specific SPB Assembly Defects; Telomere Maintenance Role; Regulates Replicative Lifespan; Ortholog Of C. Elegans Lifespan Regulator PHA-4
Protein interactions animation. Clip 10 of 10. Final clip in an animation sequence showing protein interactions within a dividing cell. This clip, which includes labels, shows an actin-myosin bundle (right) forming part of the contractile ring at the periphery of the cell. Proteins (left) are in the surrounding cytoplasm, including those that activate the contractile ring. This contraction (a form of cytokinesis) is initiated by a wave of calcium ions (see K003/3843). Here, the heads of the myosin filaments (dark) are wrapped around the actin filaments (light) and pulling them. The full sequence of ten clips shows the interaction between the protein calmodulin (CaM, calcium-modulated protein), calcium ions, the MLCK (myosin light-chain kinase) protein, and the actin-myosin bundles of the cells cytoskeleton, resulting in contraction of the membrane and cell division. For the entire sequence, see clips K003/3847 to K003/3838. For the same sequence as an anaglyph 3D animation, see clips K003/4492 to K003
Authors: Bertini, Ivano; Luchinat, Claudio; Parigi, Giacomo; Yuan, Jing. Citation: Bertini, Ivano; Kursula, Petri; Luchinat, Claudio; Parigi, Giacomo; Vahokoski, Juha; Wilmanns, Matthias; Yuan, Jing. Accurate Solution Structures of Proteins from X-ray Data and a Minimal Set of NMR Data: Calmodulin-Peptide Complexes As Examples J. Am. Chem. Soc. 131, 5134-5144 (2009).. Assembly members: ...
SWISS-MODEL Template Library (SMTL) entry for 2kdu.1. Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode
Calmodulin (CaM) is a ubiquitous calcium-binding protein responsible for the binding and activation of a vast number of enzymes and signaling pathways. It contains two lobes that bind two calcium ions each, separated by a flexible central linker. This structural flexibility allows CaM to bind and regulate a large number of diverse protein targets within the cell in response to Ca2+ gradients. Voltage gated calcium channels (CaVs), as main sources of extracellular Ca2+, are crucial for a number of physiological processes, from muscle contraction to neurotransmission and endocrine function. These large transmembrane proteins open in response to membrane depolarization and allow gated entry of Ca2+ ions into the cytoplasm. Their regulation is currently the subject of intense investigation due to its pharmacological and scientific importance. CaM has been previously shown to pre-associate and act as a potent inhibitor of one class of high-voltage activated (HVA) channels called L-type channels via ...
In the first PCR reaction, both N- and C-terminal fragments were amplified separately and purified after electrophoresis on an agarose gel. These two fragments shared an overlapping region of at least 18 bp containing the mutations at position 92, so that in a second PCR reaction both fragments were mixed and the whole fragment was amplified with CMD1N+ and CMD1C− primers. The fragment containing the mutation was digested with BstBI and SphI, and was subcloned into the BstBI-SphI gap of pRB1616. All mutations were verified by DNA sequencing. DNA sequencing with two sequencing primers (5″-TGACCGGAAACTACTGAAC-3″ and 5″-GATGAACGAAATAGATGTTGATGG-3″) sufficed to cover the entire coding sequence of calmodulin.. Construction of yeast strains: To integrate cmd1 mutations into the genome, we used the pRB1617-derived plasmids (using HIS3 as a selectable marker) or pRB1617L-derived plasmids (using LEU2 as a selectable marker). After digestion of these plasmids with SacII and AlwNI, the ...
Roles of calmodulin and CaMKII in mediating PKG stimulation of Kir6.2/SUR2A channels.Recombinant Kir6.2/SUR2A channels were expressed in HEK293 cells by transie
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Background CALM2 is the second calmodulin gene. Although the CALM1,CALM2, and CALM3 calmodulin proteins are identical, at the nucleotide level they share only about 80% identity within their coding regions, and they contain...
Ca(2+)-dependent inactivation (CDI) of L-type Ca(2+) channels plays a critical role in controlling Ca(2+) entry and downstream signal transduction in excitable cells. Ca(2+)-insensitive forms of calmodulin (CaM) act as dominant negatives to prevent CDI, suggesting that CaM acts as a resident Ca(2+) sensor. However, it is not known how the Ca(2+) sensor is constitutively tethered. We have found that the tethering of Ca(2+)-insensitive CaM was localized to the C-terminal tail of alpha(1C), close to the CDI effector motif, and that it depended on nanomolar Ca(2+) concentrations, likely attained in quiescent cells. Two stretches of amino acids were found to support the tethering and to contain putative CaM-binding sequences close to or overlapping residues previously shown to affect CDI and Ca(2+)-independent inactivation. Synthetic peptides containing these sequences displayed differences in CaM-binding properties, both in affinity and Ca(2+) dependence, leading us to propose a novel mechanism for ...
View mouse Camta1 Chr4:151059525-151861876 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
The Ca2+-activated Cl channel anoctamin-1 (Ano1; Tmem16A) plays a variety of physiological roles, including epithelial fluid secretion. Ano1 is activated by increases in intracellular Ca2+, but there is uncertainty whether Ca2+ binds directly to Ano1 or whether phosphorylation or additional Ca2+-binding subunits like calmodulin (CaM) are required. Here we show that CaM is not necessary for activation of Ano1 by Ca2+ for the following reasons. (a) Exogenous CaM has no effect on Ano1 currents in inside-out excised patches. (b) Overexpression of Ca2+-insensitive mutants of CaM have no effect on Ano1 currents, whereas they eliminate the current mediated by the small-conductance Ca2+-activated K+ (SK2) channel. (c) Ano1 does not coimmunoprecipitate with CaM, whereas SK2 does. Furthermore, Ano1 binds very weakly to CaM in pull-down assays. (d) Ano1 is activated in excised patches by low concentrations of Ba2+, which does not activate CaM. In addition, we conclude that reversible ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
I need an online or downloadable hydropathy plot programme. But I need something special! I want a programme that takes into account the presence or absence of non-covalent modifications, especially phosphorylation sites and calmodulin binding sites. Any suggestions? If so, please email me at: o.s.depeyer at reading.ac.uk ...
85. Assessment of Foreign Qualifications Act, cf. Consolidation Act No. 74 of 24 January 2003, with the amendments following from Act No. 315 of 30 March 2007, (2007).. ...
Myc-DDK-tagged ORF clone of Homo sapiens calmodulin-like 4 (CALML4), transcript variant 1 as transfection-ready DNA - 10 µg - OriGene - cdna clones
Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein.
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TY - JOUR. T1 - Phosphorylation of smooth muscle myosin light chain kinase by Ca2+/calmodulin-dependent protein kinase II. T2 - Comparative study of the phosphorylation sites. AU - Hashimoto, Yoshiaki. AU - Soderling, Thomas. PY - 1990. Y1 - 1990. N2 - Smooth muscle myosin light chain kinase (MLC-kinase) was rapidly phosphorylated in vitro by the autophosphorylated form of Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II) to a molar stoichiometry of 2.77 ± 0.15 associated with a threefold increase in the concentration of calmodulin (CaM) required for half-maximal activation of MLC-kinase. Binding of CaM to MLC-kinase markedly reduced the phosphorylation stoichiometry to 0.21 ± 0.05 and almost completely inhibited phosphorylation of sites in two peptides (32P-peptides P1 and P2) with reduced phosphorylation of peptide P3. By analogy, cAMP-dependent protein kinase phosphorylated MLC-kinase to a stoichiometry of 3.0 or greater in the absence of CaM with about a threefold decrease in the ...
TY - JOUR. T1 - Definition of the Inhibitory Domain of Smooth Muscle Myosin Light Chain Kinase by Site-Directed Mutagenesis. AU - Ito, Masaaki. AU - Guerriero, Vince. AU - Chen, Xiaomin. AU - Hartshorne, David J.. PY - 1991/4/1. Y1 - 1991/4/1. N2 - Site-directed mutagenesis of smooth muscle myosin light chain kinase was applied to define its autoinhibitory domain. Mutants were all initiated at Leu-447 but contained varying lengths of C-terminal sequence. Those containing the complete C-terminal sequence to Glu-972 possessed kinase activities that were calmodulin-dependent. Removal of the putative inhibitory domain by truncation to Thr-778 resulted in generation of a constitutively active (calmodulin-independent) species. Thus, the inhibitory domain lies to the C-terminal side of Thr-778. Truncation to Lys-793 and to Trp-800 also resulted in constitutively active mutants, although the specific activity of the latter was less than the other mutants. None of the truncated mutants bound calmodulin. ...
The prediction of calmodulin-binding (CaM-binding) proteins plays a very important role in the fields of biology and biochemistry, because the calmodulin protein binds and regulates a multitude of protein targets affecting different cellular processes. Computational methods that can accurately identify CaM-binding proteins and CaM-binding domains would accelerate research in calcium signaling and calmodulin function. Short-linear motifs (SLiMs), on the other hand, have been effectively used as features for analyzing protein-protein interactions, though their properties have not been utilized in the prediction of CaM-binding proteins. We propose a new method for the prediction of CaM-binding proteins based on both the total and average scores of known and new SLiMs in protein sequences using a new scoring method called sliding window scoring (SWS) as features for the prediction module. A dataset of 194 manually curated human CaM-binding proteins and 193 mitochondrial proteins have been obtained and used
Fingerprint Dive into the research topics of Interaction of Calmodulin with Skeletal Muscle Myosin Light Chain Kinase. Together they form a unique fingerprint. ...
We report the identification and characterization of myr 4 (myosin from rat), the first mammalian myosin I that is not closely related to brush border myosin I. Myr 4 contains a myosin head (motor) domain, a regulatory domain with light chain binding sites and a tail domain. Sequence analysis of myosin I head (motor) domains suggested that myr 4 defines a novel subclass of myosin Is. This subclass is clearly different from the vertebrate brush border myosin I subclass (which includes myr 1) and the myosin I subclass(es) identified from Acanthamoeba castellanii and Dictyostelium discoideum. In accordance with this notion, a detailed sequence analysis of all myosin I tail domains revealed that the myr 4 tail is unique, except for a newly identified myosin I tail homology motif detected in all myosin I tail sequences. The Ca(2+)-binding protein calmodulin was demonstrated to be associated with myr 4. Calmodulin binding activity of myr 4 was mapped by gel overlay assays to the two consecutive light ...
The effect of calmodulin on the order of lipids in rhodopsin-free and rhodopsin-containing membranes has been studied using spin-label electron spin resonance methods. Calmodulin, up to 10(-6)M, did not change the measured order of lipids in bilayer membranes containing only rhodopsin. However, for bovine rod outer segment disc membranes, which contain rhodopsin and other proteins, calmodulin induced a significant concentration and temperature dependent increase in the order of the membrane lipids. This suggests that the site of calmodulin binding is remote from rhodopsin itself, and the nature of the binding appears to be a membrane surface phenomenon.
The Munc13 proteins are the key mediators of synaptic vesicle priming, an essential step in Ca2+-regulated neurotransmitter release that renders docked vesicles fusion-competent prior to exocytosis. They have emerged as important regulators of adaptive synaptic mechanisms such as presynaptic short-term plasticity, a process by which the release of neurotransmitter is dynamically adapted to a changing demand. Indeed, Munc13-1 and ubMunc13-2 contain a conserved calmodulin (CaM) binding site and the Ca2+-dependent interaction of these Munc13 isoforms with CaM constitutes a molecular mechanism that transduces residual Ca2+ signaling to the synaptic exocytotic machinery. This study aimed to (i) establish whether such regulation through CaM exists in the other Munc13 isoforms, bMunc13-2 and Munc13-3, and (ii) provide structural insights into the Munc13-CaM interaction. Bioinformatic tools were used to identify potential CaM recognition motifs in the non-conserved sequences of bMunc13-2 and Munc13-3. ...
TY - JOUR. T1 - Structural organization, DNA sequence, and expression of the calmodulin gene. AU - Zimmer, W. E.. AU - Schloss, J. A.. AU - Silflow, C. D.. AU - Youngblom, J.. AU - Watterson, D. M.. N1 - Copyright: Copyright 2004 Elsevier B.V., All rights reserved.. PY - 1988. Y1 - 1988. N2 - Calmodulin is encoded in Chlamydomonas reinhardtii by a single gene that 1) has multiple intervening sequences, 2) has 5 structural motifs that are phylogenetically conserved, 3) contains 5 sequences that are similar to those found in genes of some transforming, cytoskeletal, and stress-response proteins, and 4) produces at both life cycle stages, a single size class of mRNA and proteins that are identical in amino acid sequence. Based on the amino acid sequence of calmodulin from the vegetative phase of the life cycle, synthetic oligonucleotide probes, containing inosine in order to reduce codon redundancy, were used to detect and isolate cloned cDNAs coding for the gametic phase calmodulin. The complete ...
Changes in calmodulin (CaM) mRNA and protein were investigated in aleurone layers of barley (Hordeum vulgare L. cv Himalaya) incubated in the presence and absence of calcium, gibberellic acid (GA3), and abscisic acid (ABA). CaM mRNA levels increased rapidly and transiently following incubation of aleurone layers in H2O, CaCl2, or GA3. The increase in CaM mRNA was prevented by ABA. This increase in CaM mRNA was brought about by physical stimulation during removal of the starchy endosperm from the aleurone layer. CaM protein levels did not increase in response to physical stimulation. Only incubation in GA3 plus CaCl2 brought about a rapid increase in CaM protein levels in the aleurone cell. ABA reduced the level of CaM protein below that found at the beginning of the incubation period. The rise in CaM protein preceded increases in the synthesis and secretion of [alpha]-amylase. Immunocytochemistry with monoclonal antibodies to carrot and mung bean CaM was used to localize CaM in aleurone ...
TY - JOUR. T1 - Degradation of PEP-19, a calmodulin-binding protein, by calpain is implicated in neuronal cell death induced by intracellular Ca2+ overload. AU - Kanazawa, Y.. AU - Makino, M.. AU - Morishima, Y.. AU - Yamada, K.. AU - Nabeshima, T.. AU - Shirasaki, Y.. PY - 2008/6/23. Y1 - 2008/6/23. N2 - Excessive elevation of intracellular Ca2+ levels and, subsequently, hyperactivation of Ca2+/calmodulin-dependent processes might play an important role in the pathologic events following cerebral ischemia. PEP-19 is a neuronally expressed polypeptide that acts as an endogenous negative regulator of calmodulin by inhibiting the association of calmodulin with enzymes and other proteins. The aims of the present study were to investigate the effect of PEP-19 overexpression on cell death triggered by Ca2+ overload and how the polypeptide levels are affected by glutamate-induced excitotoxicity and cerebral ischemia. Expression of PEP-19 in HEK293T cells suppressed calmodulin-dependent signaling and ...
Unloaded shortening velocity, a mechanical parameter associated with the rate of cross-bridge cycling, was investigated in chemically skinned guinea pig taenia coli and hog carotid artery. Shortening velocity was measured by the technique described by Edman, whereby large length steps are rapidly imposed on the muscle and the time under unloaded conditions is determined from the isometric myograms. Shortening velocity determined in this manner was similar to Vmax from the Hill force-velocity relations reported for both living and skinned taenia coli, and, in the case of carotid artery, was at least as large as that reported for living muscle. The behavior of shortening velocity was qualitatively similar for both preparations. Shortening velocity was strongly temperature dependent, with a Q10 of approximately 3.6. Shortening velocity was found to be dependent on both the Ca++ and calmodulin concentration. In contrast to the dependence of isometric force on Ca++-calmodulin, shortening velocity ...
Fingerprint Dive into the research topics of Role of cardiac ryanodine receptor calmodulin-binding domains in mediating the action of arrhythmogenic calmodulin N-domain mutation N54I. Together they form a unique fingerprint. ...
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DNA-binding activity of a maize heat shock transcription factor (HSF) was induced by heat shock of a whole cell extract at 44°C. Addition of the calcium ion chelator EGTA reduced the binding of the HSF to heat shock element (HSE) in vitro. Re-addition of CaCl2 to the sample pretreated with EGTA restored the ability of the HSF to bind to DNA. DNA-binding activity of the HSF was also induced by directly adding CaCl2 to a whole cell extract at non-heat-shock temperature, but not by MgCl2. During HS at 44°C, calmodulin (CaM) antagonists chlorpromazine (CPZ) and N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W7) inhibited DNA-binding activity of the HSF in a concentration-dependent manner, but N-(6-aminohexyl)-1-naphthalenesulfonamide (W5), an inactive structural analogue of W7, did not. Addition of antiserum specific to CaM reduced the binding of the HSF to HSE. Re-addition of CaM to the sample pretreated with antiserum could restore the binding activity of the HSF. DNA-binding activity of ...
Molecular dynamics (MD) simulation techniques have been employed to investigate structure and function relationships in cell motility proteins at atomic resolution. (1) To analyze motions in cell motility proteins an algorithm is described to identify and visualize the movements of rigid domains about common hinges in proteins. In comparing two structures, the method partitions a protein into domains of preserved geometry and characterizes the relative movement of domains by effective rotation axes. (2) Simulated in solution, the calcium-binding protein calmodulin exhibits large conformational changes on the nanosecond time scale. The central a-helix, which has been shown to unwind locally upon binding of calmodulin to target proteins, bends and unwinds near residue Arg74. The major structural change is a reorientation of the two Ca2+-binding domains with respect to each other and a rearrangement of α-helices in the N-terminus domain which make the hydrophobic target peptide binding site more ...
Problem statement: The present study was performed to determine the effect of Intracerebroventricular (ICV) administration of W-7, a specific calmodulin inhibitor, on the analgesic effect and development of tolerance to antinociceptive effect of acute and chronic morphine administration respectively. Approach: This study was carried out on male wistar rats, weighing 200-250 g. For acute experimental protocol, Morphine was injected intraperitonealy in a single dose (5 mg kg-1). For chronic experimental protocol, Morphine was administered daily (15 mg kg-1 for 8 days). The threshold to thermal nociceptive stimuli was measured by tail-flick test. In acute and chronic experiments, W-7 (0.25, 0.5 and 1 μmol/rat) was injected through ICV at different paradigms. Maximal Possible Effect percentage (MPE%) was considered as analgesia index. Results: Our result showed that W-7 (0.25, 0.5 and 1 μmol/rat) injections before acute morphine administration significantly reduced the analgesic effect of
We investigated the effects of Wenxin Keli (WXKL) on the Calcium/Calmodulin dependent kinase II (CaMK II) signal transduction pathway with transverse aortic constriction (TAC) rats. Echocardiographic measurements were obtained 3 and 9 weeks after the surgery. Meanwhile, the action potentials (APDs) were recorded using the whole-cell patch clamp technique, and western blotting was used to assess components of the CaMK II signal transduction pathway. At both 3 and 9 weeks after treatment, the fractional shortening (FS%) increased in the WXKL group compared with the TAC group. The APD|sub|90|/sub| of the TAC group was longer than that of the Sham group and was markedly shortened by WXKL treatment. Western blotting results showed that the protein expressions of CaMK II, phospholamban (PLB), and ryanodine receptor 2 (RYR2) were not statistically significant among the different groups at both treatment time points. However, WXKL treatment decreased the protein level and phosphorylation of CaMK II (Thr
Sequence searching (5) revealed that 14 of the 39 calmodulin-binding proteins contain a motif whose consensus is (I/L)QXXK(K/X)GB, where X is any residue and B is a basic residue (Fig. 2B). A related sequence in myosins, IQXXXXKXXXR, has been shown previously to bind calmodulin (18). Thus, we demonstrate that the domain is found in many calmodulin-binding proteins. Presumably the other targets that lack this motif have other calmodulin-binding sequences (10).. In addition to the calmodulin-binding targets, we also identified one protein, Pyc1p, that bound Cy3-labeled streptavidin. Pyc1p encodes a pyruvate carboxylase 1 homolog that contains a highly conserved biotin attachment region (19). Thus, as predicted by its sequence, Pyc1p is biotinylated in vivo. With appropriate detection assays, we expect that proteome chips can identify many types of posttranslational modification of proteins.. To test whether proteome chips could be used to identify activities that might not be accessible by other ...
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David Yue and colleagues report in the the current issue of Cell a surprising role for Ca2+-unbound apopcalmodulin in regulating calcium and sodium channel activities. The Ca2+-free form of calmodulin (apoCaM) often appears inert, modulating target molecules only upon conversion to its Ca2+-bound form. This schema has appeared to govern voltage-gated Ca2+ channels, where apoCaM has been considered a dormant Ca2+ sensor, associated with channels but awaiting the binding of Ca2+ ions before inhibiting channel opening to provide vital feedback inhibition. Using single-molecule measurements of channels and chemical dimerization to elevate apoCaM, we find that apoCaM binding on its own markedly upregulates opening, rivaling the strongest forms of modulation. Upon Ca2+ binding to this CaM, inhibition may simply reverse the initial upregulation. As RNA-edited and -spliced channel variants show different affinities for apoCaM, the apoCaM-dependent control mechanisms may underlie the functional diversity ...
Activation-induced cytidine deaminase (AID) is the key mutagenic enzyme that initiates somatic hypermutation (SH) and class switch recombination (CSR) by deaminating cytosine to uracil. The targeting of AID and therefore SH and CSR to Ig genes is a central process of the immune system, but the trans-acting factors mediating the specific targeting have remained elusive. Here we show that defective calmodulin inhibition of the transcription factor E2A after activation of the B cell receptor (BCR) leads to reduced BCR, IL4 plus CD40 ligand stimulated CSR to IgE and instead CSR to other Ig classes. AID that initiates CSR is shown to be in a complex with the transcription factors E2A, PAX5 and IRF4 on key sequences of the Igh locus. Calmodulin shows proximity with each of them after BCR stimulation. BCR signaling reduces binding of the proteins to some of the target sites on the Igh locus, and calmodulin resistance of E2A blocks these reductions. AID binds directly to the bHLH domain of E2A and to ...
Calcium-calmodulin (CaM) binding to the epidermal growth factor receptor (EGFR) has been shown to both inhibit and stimulate receptor activity. CaM binds to the intracellular juxtamembrane (JM) domain (Met645-Phe688) of EGFR. Protein kinase C (PKC) mediated phosphorylation of Thr654 occurs within this domain. CaM binding to the JM domain inhibits PKC phosphorylation and conversely PKC mediated phosphorylation of Thr654 or Glu substitution of Thr654 inhibits CaM binding. A second threonine residue (Thr669) within the JM domain is phosphorylated by the mitogen-activated protein kinase (MAPK). Previous results have shown that CaM interferes with EGFR-induced MAPK activation. If and how phosphorylation of Thr669 affects CaM-EGFR interaction is however not known.In the present study we have used surface plasmon resonance (BIAcore) to study the influence of Thr669 phosphorylation on real time interactions between the intracellular juxtamembrane (JM) domain of EGFR and CaM. The EGFR-JM was expressed as ...
Background Calmodulin (CaM) plays an important role in Ca2+-dependent signal transduction. Ca2+ binding to CaM triggers a conformational change, forming a hydrophobic patch that is important for target protein recognition. CaM regulates a Ca2+-dependent inactivation process in store-operated Ca2+entry, by interacting Orai1. To understand the relationship between Ca2+-induced hydrophobicity and CaM/Orai interaction, chimera proteins constructed by exchanging EF-hands of CaM with those of Troponin C (TnC) are used as an informative probe to better understand the functionality of each EF-hand. Results ANS was used to assess the context of the induced hydrophobic surface on CaM and chimeras upon Ca2+ binding. The exchanged EF-hands from TnC to CaM resulted in reduced hydrophobicity compared with wild-type CaM. ANS lifetime measurements indicated that there are two types of ANS molecules with rather distinct fluorescence lifetimes, each specifically corresponding to one lobe of CaM or chimeras.
The effect of Ca2+ and calmodulin on phosphorylation of islet secretory granule proteins was studied. Secretory granules were incubated in a phosphorylation reaction mixture containing [32P]ATP and test reagents. The 32P-labeled proteins were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the 32P content was visualized by autoradiography, and the relative intensities of specific bands were quantitated. When the reaction mixture contained EGTA and no added Ca2+, 32P was incorporated into two proteins with molecular weights of 45,000 and 13,000. When 10−4 M Ca2+ was added without EGTA, two additional proteins (58,000 and 48,000 Mr) were phosphorylated, and the 13,000-Mr protein was absent. The addition of 2.4 μM calmodulin markedly enhanced the phosphorylation of the 58,000- and 48,000-Mr proteins and resulted in the phosphorylation of a major protein whose molecular weight (64,000 Mr) is identical to that of one of the calmodulin binding proteins located on the granule ...
BACKGROUND: In contrast to conventional muscle myosins, where two different light chains (LCs) stabilize the elongated regulatory domain (RD) region of the head portion of the molecule, unconventional myosins are a diverse group of motors in which from one to six calmodulin (CaM) subunits are bound tandemly to the RD. In both cases, the heavy chains of the RDs have special sequences called IQ motifs to which the LCs or CaM bind. A previously puzzling aspect of certain unconventional myosins is their unusual mode of regulation, where activation of motility occurs at low levels of Ca2+. Although the atomic structure of the conventional muscle myosin RD has been determined, no crystallographic structure of the RD of an unconventional myosin is yet available. RESULTS: We have constructed a model of vertebrate CaM bound to the first IQ motif present in the neck region of an unconventional myosin (chicken brush border myosin I), using strict binding rules derived from the crystal structure of the ...
Numerous investigations reported that increases of internal Ca2+ (Ca2+i) pivotally regulate high voltage-activated (HVA) Ca2+ channels via calmodulin (CaM). However, it is largely elusive that Ca2+i can regulate low voltage-activated T-type Ca2+ channels. Using whole cell patch clamp, we compared the biophysical properties of Ca2+ current through T-type Ca2+ channel Cav3.1, Cav3.2, or Cav3.3 stably expressed in HEK293 cells between internal solutions containing 27 nM and l μM free Ca2+. Both activation and inactivation kinetics of Cav3.3 current in l μM Ca2+i solution were more rapid than those of Cav3.3 in 27 nM Ca2+i solution. In addition, both activation and steady-state inactivation curves of Cav3.3 were negatively shifted in the higher Ca2+i solution. In contrast, the biophysical properties of Cav3.1 and Cav3.2 isoforms were not different between the two internal solutions. Overexpression of CaM1234 (calmodulin mutant lacking 4 Ca2+ binding sites) strongly suppressed the effects of l μM ...
TY - JOUR. T1 - Regulation of calmodulin mRNAs in differentiating human IMR-32 neuroblastoma cells. AU - Toutenhoofd, Sonja L.. AU - Strehler, Emanuel E.. N1 - Funding Information: We thank Dr. A. Marc Gacy for help with statistical data analysis and for critical reading of the manuscript. This work was supported in part by a grant from the Fraternal Order of Eagles Cancer Research Fund (Eagles #176), by the Mayo Clinic Cancer Center, and the Mayo Foundation for Medical Education and Research.. PY - 2002/11/4. Y1 - 2002/11/4. N2 - Calmodulin (CaM), the principal mediator of the calcium signal, regulates numerous processes pertinent to neural function. Mammalian CaM is generated from three genes that give rise to five distinct transcripts. To determine the regulation of individual CaM transcripts in neurons, we assessed their abundance during differentiation of human IMR-32 neuroblastoma cells. Northern analysis revealed that the 4.1 kb CALM1 transcript was specifically upregulated about ...
A number of mouse and rat cells and their virus-transformed counterparts were tested for sensitivity to Pseudomonas aeruginosa exotoxin A (PEA). In each case, the transformed cells were considerably less sensitive than were the nontransformed cells. In the presence of trifluoperazine, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, or retinoic acid, the transformed cells became as sensitive as the nontransformed cells, whereas these drugs had little or no effect on the sensitivity to PEA of the nontransformed cells. Temperature-sensitive virus-transformed normal rabbit kidney cells were sensitized to PEA by N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, when these cells were grown as the transformed phenotype, whereas the nontransformed phenotype could not be sensitized. The possibility is discussed that upon malignant transformation a process which is dependent upon calmodulin or protein kinase C strongly decreases the sensitivity of the cells to PEA.. ...
Read Two isoforms of glutamate decarboxylase in Arabidopsis are regulated by calcium/calmodulin and differ in organ distribution, Plant Molecular Biology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
TY - CHAP. T1 - Biochemistry and Pharmacology of Calmodulin-Regulated Phosphatase Calcineurin. AU - Perrino, Brian A.. AU - Soderling, Thomas R.. PY - 2012/12/2. Y1 - 2012/12/2. UR - http://www.scopus.com/inward/record.url?scp=84941124499&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=84941124499&partnerID=8YFLogxK. U2 - 10.1016/B978-0-08-092636-0.50008-6. DO - 10.1016/B978-0-08-092636-0.50008-6. M3 - Chapter. AN - SCOPUS:84941124499. SN - 9780127138602. SP - 169. EP - 236. BT - Calmodulin and Signal Transduction. PB - Elsevier Inc.. ER - ...
A short synthetic peptide (Pa) containing a structural motif (2-6-11 motif) present in a number of human extracellular matrix proteins was found to stimulate the production of cytokines IL-1alpha, IL-1beta, IL-6, and TNFalpha by human peripheral blood mononuclear cells. We have now investigated the signal transduction pathway involved in the elicitation of these immunomodulating properties on isolated human monocytes.. Our results show that active peptide Pa provoked phosphoinositide hydrolysis, intracellular calcium elevation, and cAMP accumulation. Herbimycin A, an inhibitor of protein tyrosine kinases (PTK), markedly reduced these effects of peptide Pa. We have also found that this peptide stimulated CREB, NF-kappaB, and AP-1 DNA-binding activity.. With the help of inhibitors of PTK (herbimycin A), phospholipase C (neomycin sulfate), protein kinase C (bis-indolyl maleimide), protein kinase A (H89), and the calmodulin antagonist W-7, as well as cholera toxin, an agent that increases ...
Typically hippocampal long-term potentiation (LTP) of synaptic strength requires Ca2+/calmodulin(CaM)-dependent Bibf1120 protein kinase II Bibf1120 (CaMKII) and Bibf1120 other kinases while long-term depression (LTD) requires phosphatases. This differential rules triggered GluA1 S831 to become well-liked by LTP-type stimuli (solid but short) while GluA1 S567 was well-liked by LTD-type stimuli (fragile but long term). Thus dependence on autonomous CaMKII in opposing types of plasticity requires specific substrate classes that are differentially controlled to allow stimulus-dependent substrate-site choice. Intro LTD and LTP trigger long-term adjustments Bibf1120 of synaptic power in reverse directions; both are Ca2+- reliant may appear at the same hippocampal CA3 to CA1 synapses and so are together considered to underlie learning memory space and cognition (for review discover (Collingridge et al. 2010 Carry and Malenka 2004 Martin et al. 2000 Xia and Surprise 2005 Twenty-five many years of study ...
Product Name: Calmodulin, Wheat (Triticum aestivum), FluoresceinFormula: MW: 16,750 DaAppearance: LyophilizedMedchemexpressPurity: 98% by SDS-PAGESpecification:
When membrane potential is depolarized, intracellular Ca2+ beneath the plasma membrane of cardiac myocytes increases. Ca2+ binds to CaM and Ca2+/CaM complex leads to the facilitation of RGS action to accelerate hydrolysis of GKα-GTP to GKα-GDP. GKα-GDP binds free Gβγ to form trimeric G proteins, which therefore decreases the number of free Gβγ and thus the number of available KG channels at depolarized potentials. The time-dependent increase in KG current on hyperpolarization can then be interpreted as the reflection of the reverse reactions of these events, ie, less Ca2+ influx, less Ca2+/CaM, lesser activity of RGS, and more available Gβγ.. There still remain, however, two major questions in this reaction scheme. The first one is how Ca2+/CaM facilitates RGS action. It was reported that Ca2+/CaM binds RGS but does not change its GTPase accelerating activity in vitro.14 Therefore, some mechanisms other than direct facilitating action of Ca2+/CaM on the GTPase-accelerating function of ...
Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
The effects of extracellularly applied 3′-5′ cyclic guanosine monophosphate (cGMP) on kainate responses from cultured cerebellar granule and Purkinje neurons were investigated using whole-cell and outside-out patch recording modes. Cerebellar granule cell responses to kainate were not homogeneous, nor were the effects of cGMP. Therefore, effects of cGMP are described for two groups of granule cells categorized on the basis of the underlying channel conductance estimated by variance analysis. Cells with high-noise kainate responses had average channel conductances of 5 to 7 picoseimens, whereas the average conductances of low-variance noise responses were 0.3 to 2.0 picoseimens. High-noise kainate responses were inhibited by externally applied cGMP (5-1000 μM) in a rapidly reversible and dose-dependent manner. IC50 values were estimated at ∼150 μM cGMP for 25 μM kainate and ∼500 μM cGMP for 100 μM kainate. Evidence that cGMP-mediated inhibition of high-noise kainate responses ...
Ubiquitination was surprising because tBid-N has no lysine residues that conventionally act as ubiquitin acceptor sites (Fig. S1 B). Typically, ubiquitin can be linked either via a peptide bond to the ε amino group of a lysine residue or to the α amino group of an N-terminal residue (Ciechanover and Ben-Saadon, 2004). Because linkage to lysine was excluded, we investigated whether the N terminus of tBid-N acted as a ubiquitin acceptor site. To this end, tBid-N was fused C-terminally to a tandem affinity purification (TAP) tag, which contains a calmodulin-binding domain and protein A sequence separated by a tobacco etch virus (TEV) protease-sensitive site (ENLYFQG). This allows for two-step purification; first on IgG beads and then after cleavage by TEV on calmodulin beads (Rigaut et al., 1999). In one tBid-N TAP construct (TEV tBid-N TAP 7), sequences encoding the first seven amino acids of tBid-N and a TEV protease site were cloned upstream of the tBid-N coding region (Fig. 3 C). If tBid-N ...
AMPK can also be activated by a Ca2+-mediated pathway involving phosphorylation at Thr-172 by the Ca2+/calmodulin-dependent protein kinase, CaMKK 3. CaMKKa and CaMKK 3 were discovered as the upstream kinase for the calmodulin-dependent protein kinases-1 and -IV they both activate AMPK in a Ca2+/ calmodulin-dependent manner in cell-free assays, although CaMKK 3 appears to much more active against AMPK in intact cells. Expression of CaMKKa and CaMKK(3 primarily occurs in neural tissues, but CaMKKp is also expressed in some other cell types. Thus, the Ca2+-mediated pathway for AMPK activation has now been shown to occur in response to depolarization in rat neuronal tissue, in response to thrombin (acting via a Gq-coupled receptor) in endothelial cells, and in response to activation of the T cell receptor in T cells. [Pg.71] ...
Glioblastoma multiforme is a fatal malignancy of the central nervous system, demanding new methods of treatment. The combination of a calmodulin antagonist with bleomycin has shown synergistic activity in several preclinical models and has been evaluated in a Phase I clinical trial. Since phenothiazines reach high concentrations in the central nervous system, and bleomycin has been reported to have antitumoral activity as well, we studied this combination in a Phase II clinical trial. In addition, we purified calmodulin from normal brain and malignant gliomas to determine its biochemical and pharmacological characteristics. Seventeen patients were entered onto this study and all were evaluable. There were no partial or complete responses. There was one case of fatal pulmonary toxicity in a patient showing an objective tumor response. Otherwise, the treatment was well tolerated. Calmodulin purified from the normal brain and gliomas of patients undergoing resection was identical to each other and ...
We identified and analyzed 33 and 29 IQD1-like genes in Arabidopsis thaliana and Oryza sativa, respectively. The encoded IQD proteins contain a plant-specific domain of 67 conserved amino acid residues, referred to as the IQ67 domain, which is characterized by a unique and repetitive arrangement of three different calmodulin recruitment motifs, known as the IQ, 1-5-10, and 1-8-14 motifs. We demonstrated calmodulin binding for IQD20, the smallest IQD protein in Arabidopsis, which consists of a C-terminal IQ67 domain and a short N-terminal extension. A striking feature of IQD proteins is the high isoelectric point (~10.3) and frequency of serine residues (~11%). We compared the Arabidopsis and rice IQD gene families in terms of gene structure, chromosome location, predicted protein properties and motifs, phylogenetic relationships, and evolutionary history. The existence of an IQD-like gene in bryophytes suggests that IQD proteins are an ancient family of calmodulin-binding proteins and arose ...
We identified and analyzed 33 and 29 IQD1-like genes in Arabidopsis thaliana and Oryza sativa, respectively. The encoded IQD proteins contain a plant-specific domain of 67 conserved amino acid residues, referred to as the IQ67 domain, which is characterized by a unique and repetitive arrangement of three different calmodulin recruitment motifs, known as the IQ, 1-5-10, and 1-8-14 motifs. We demonstrated calmodulin binding for IQD20, the smallest IQD protein in Arabidopsis, which consists of a C-terminal IQ67 domain and a short N-terminal extension. A striking feature of IQD proteins is the high isoelectric point (~10.3) and frequency of serine residues (~11%). We compared the Arabidopsis and rice IQD gene families in terms of gene structure, chromosome location, predicted protein properties and motifs, phylogenetic relationships, and evolutionary history. The existence of an IQD-like gene in bryophytes suggests that IQD proteins are an ancient family of calmodulin-binding proteins and arose ...
Benaim G, Villalobo A (August 2002). "Phosphorylation of calmodulin. Functional implications". European Journal of Biochemistry ...
Application to calmodulin". Biochemistry. 29 (19): 4659-67. doi:10.1021/bi00471a022. PMID 2372549. Lewis E Kay; Mitsuhiko Ikura ...
Benaim G, Villalobo A (August 2002). "Phosphorylation of calmodulin. Functional implications" (PDF). European Journal of ...
Reis, J. (2011). Video: Calmodulin Synthesis ; Lisbon Ensemble 20/21 ; M.: Pedro Pinto Figueiredo; Marco Fernandes, Miguel ... 2 percussionists 2003/2004 Phonopolis Electronics 2003 Síntese Orchestra 2003 Lysozyme Synthesis Piano 2002 Calmodulin ... Retrieved from https://itunes.apple.com/pt/album/portuguese-contemporary-music/id957574297 Reis, J. (2016). Calmodulin ...
Calmodulin participates in an intracellular signaling system by acting as a diffusible second messenger to the initial stimuli ... Pb2+ (lead) can replace Ca2+ (calcium) as, for example, with calmodulin or Zn2+ (zinc) as with metallocarboxypeptidases Some ... Chin D, Means AR (August 2000). "Calmodulin: a prototypical calcium sensor". Trends in Cell Biology. 10 (8): 322-8. doi:10.1016 ... Stevens FC (August 1983). "Calmodulin: an introduction". Canadian Journal of Biochemistry and Cell Biology. 61 (8): 906-10. doi ...
Benaim G, Villalobo A (Aug 2002). "Phosphorylation of calmodulin. Functional implications". European Journal of Biochemistry / ...
Application to calmodulin". Biochemistry. 29 (19): 4659-67. doi:10.1021/bi00471a022. PMID 2372549. Lewis E Kay; Mitsuhiko Ikura ...
Cook WJ, Walter LJ, Walter MR (1995). "Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex". ... 1993). "Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin ... "Functional analysis of the promoters of the human CaMIII calmodulin gene and of the intronless gene coding for a calmodulin- ... Calmodulin 3 is a protein that in humans is encoded by the CALM3 gene. GRCh38: Ensembl release 89: ENSG00000160014 - Ensembl, ...
This domain binds calmodulin, a protein known as a calcium sensor that can bind and regulate many target proteins. A GRD ( ... Hart MJ, Callow MG, Souza B, Polakis P (Aug 1996). "IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a ... Li Z, Sacks DB (February 2003). "Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1". J. Biol. Chem. 278 ... Li Z, Kim SH, Higgins JM, Brenner MB, Sacks DB (December 1999). "IQGAP1 and calmodulin modulate E-cadherin function". J. Biol. ...
For this reason protein kinases are named based on what regulates their activity (i.e. Calmodulin-dependent protein kinases). ... The 1970s included the discovery of calmodulin-dependent protein kinases and the finding that proteins can be phosphorylated on ... Activation loop Autophosphorylation Ca2+/calmodulin-dependent protein kinase Cell signaling Cyclin-dependent kinase G protein- ...
Tuberculosis toxin blocking phagosome maturation inhibits a novel Ca2!/calmodulin-PI3K hVPS34 cascade. J. Exp. Med. 198:653-659 ...
An IQ motif provides a binding site for calmodulin (CaM) or CaM-like proteins. LRRIQ3 is predicted to be mostly alpha-helical ... In total, there are 4 conserved domains within LRRIQ3: 3 leucine-rich repeats and 1 IQ calmodulin-binding motif. Leucine-rich ... Rhoads AR, Friedberg F (April 1997). "Sequence motifs for calmodulin recognition". FASEB J. 11 (5): 331-40. doi:10.1096/fasebj. ...
They are used in Calmodulin. Rouse, G.W.; Goffredi, S.K. & Vrijenhoek, R.C. (2004). "Osedax rubiplumus Rouse, Goffredi & ...
... produces Calmodulin inhibitors. Many of the strains of Aspergillus stromatoides have been isolated in ... "Calmodulin inhibitors from Aspergillus stromatoides". Chemistry & Biodiversity. 10 (3): 328-37. doi:10.1002/cbdv.201200321. ...
First, the calcium will bind to calmodulin. After the influx of calcium ions and the binding to calmodulin, pp60 SRC (a protein ... Kim MT, Kim BJ, Lee JH, Kwon SC, Yeon DS, Yang DK, So I, Kim KW (April 2006). "Involvement of calmodulin and myosin light chain ... On either sides of the catalytic core sit calcium ion/calmodulin binding sites. Binding of calcium ion to this domain increases ... Robinson A, Colbran R (2013). "Calcium/Calmodulin-Dependent Protein Kinases". In Lennarz W, Lane D (eds.). Encyclopedia of ...
"New nuclear functions for calmodulin". Cell Calcium. 23 (2-3): 115-21. doi:10.1016/S0143-4160(98)90109-9. PMID 9601606. ...
One such example is calmodulin. One molecule of calmodulin binds four calcium ions cooperatively. Its structure presents four ... DAPK and EGFR calmodulin binding domains interact with different calmodulin-calcium complexes". Biochimica et Biophysica Acta ( ... Babu YS, Sack JS, Greenhough TJ, Bugg CE, Means AR, Cook WJ (1985). "Three-dimensional structure of calmodulin". Nature. 315 ( ... "A general strategy to characterize calmodulin-calcium complexes involved in CaM-target recognition: ...
Joyal JL, Burks DJ, Pons S, Matter WF, Vlahos CJ, White MF, Sacks DB (November 1997). "Calmodulin activates ...
Ca2+-bound calmodulin (CaM) interacts with Cav1.3 to induce calcium-dependent inactivation (CDI). Recently, it has been shown ... but weakens the pre-binding of Ca2+-free calmodulin (apoCaM) to channels. The upshot is that CDI is continuously tuneable by ... "Calcium calmodulin and hormone secretion". Clinical Endocrinology. 23 (2): 201-18. doi:10.1111/j.1365-2265.1985.tb00216.x. PMID ...
The distinguishing feature of PDE1 as a family is their regulation by calcium (Ca2+) and calmodulin (CaM). Calmodulin has been ... either at the level of calmodulin binding sites such as compound KS505a or directly on Ca2+/calmodulin such as bepril, ... In PDE1 this region contains a calmodulin binding domain. The catalytic domains of PDE1 (and other types of PDEs) have three ... Vinpocetine was described as a specific inhibitor of basal and calmodulin-activated PDE1. This effect leads to an increase of ...
"CAMK2A calcium/calmodulin dependent protein kinase II alpha [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. ... Figure 1 shows how the presence of calcium or calmodulin allows for the activation of CAM kinases (CAMK II). All kinases have a ... CAMK, also written as CaMK, is an abbreviation for the Ca2+/calmodulin-dependent protein kinase class of enzymes. CAMKs are ... Hudmon A, Schulman H (2002-06-01). "Neuronal CA2+/calmodulin-dependent protein kinase II: the role of structure and ...
Calbindin Calmodulin Calsequestrin Kinjo, Tashi G; Schnetkamp, Paul PM. Ca2+ Chemistry, Storage and Transport in Biologic ... Those that belong to the EF-hand superfamily such as Calmodulin and Calcineurin have been linked to transcription regulation. ... The most ubiquitous Ca2+-sensing protein, found in all eukaryotic organisms including yeasts, is calmodulin. Intracellular ...
Bähler M, Rhoads A (February 2002). "Calmodulin signaling via the IQ motif". FEBS Letters. 513 (1): 107-13. doi:10.1016/S0014- ... calmodulin and dynein promote meiotic spindle rotation independently of cortical LIN-5/GPR/Galpha". Nature Cell Biology. 11 (3 ... where it regulates spindle organization and rotation by interacting with calmodulin, dynein and NuMA-related LIN-5. One mouse ...
Daube H, Billich A, Mann K, Schramm HJ (1991). "Cleavage of phosphorylase kinase and calcium-free calmodulin by HIV-1 protease ... the delta subunit is calmodulin (CALM1; MIM 114180). PHKA2 (MIM 306000) encodes the alpha subunit of liver-specific ...
2006). "Influence of calcium on the proteolytic degradation of the calmodulin-like skin protein (calmodulin-like protein 5) in ... Calmodulin-like protein 5 is a protein that in humans is encoded by the CALML5 gene. This gene encodes a novel calcium binding ... "Entrez Gene: CALML5 calmodulin-like 5". Human CALML5 genome location and CALML5 gene details page in the UCSC Genome Browser. ... Mehul B, Bernard D, Simonetti L, Bernard MA, Schmidt R (Jun 2000). "Identification and cloning of a new calmodulin-like protein ...
... calmodulin-modulated myosin light chain kinase; RAF/MEK/Mitogen-activated protein kinases; PKC/Ca2+/Calcineurin/Nuclear factor ...
The major downstream calcium effectors are the calcium-binding calmodulin protein and downstream calmodulin-dependent protein ... Calmodulin dependent kinase II was shown to be the protein responsible for converting the Ca2+ influx signal into inhibition of ... Li, Nan; Wang, Chunmei; Wu, Yanan; Liu, Xingguang; Cao, Xuetao (2009-01-30). "Ca2+/Calmodulin-dependent Protein Kinase II ... Takuwa, Noriko; Zhou, Wei; Takuwa, Yoh (1995-02-01). "Calcium, calmodulin and cell cycle progression". Cellular Signalling. 7 ( ...
... is a calmodulin binding protein. Like calponin, caldesmon tonically inhibits the ATPase activity of myosin in smooth ... This gene encodes a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and ... Sobue K, Muramoto Y, Fujita M, Kakiuchi S (Sep 1981). "Purification of a calmodulin-binding protein from chicken gizzard that ... The conserved domain of this protein possesses the binding activities to Ca++-calmodulin, actin, tropomyosin, myosin, and ...
NAD kinases in plants and sea urchin eggs have also been found to bind calmodulin. Due to the essential role of NADPH in lipid ... Epel D, Patton C, Wallace RW, Cheung WY (Feb 1981). "Calmodulin activates NAD kinase of sea urchin eggs: an early event of ... Williams MB, Jones HP (Feb 1985). "Calmodulin-dependent NAD kinase of human neutrophils". Archives of Biochemistry and ... NADK is also reportedly stimulated by calcium/calmodulin binding in certain cell types, such as neutrophils. ...
Lee CH, Della NG, Chew CE, Zack DJ (November 1996). "Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit ... Wes PD, Yu M, Montell C (November 1996). "RIC, a calmodulin-binding Ras-like GTPase". The EMBO Journal. 15 (21): 5839-48. doi: ...
Calmodulin is a small thermostable protein which has been involved in the regulation of a number of cellular activities such as ... Calmodulin is a small thermostable protein which has been involved in the regulation of a number of cellular activities such as ... Calmodulin is apparently present in all nucleated cells. High concentrations from 1-50μM have been reported from a variety of ... Vandermeers A., Vandermeers-Piret MC., Christophe J. (1982) Calmodulin. In: Swillens S., Dumont J.E. (eds) Cell Regulation by ...
Calmodulin 1 (CALM1) Calmodulin 2 (CALM2) Calmodulin 3 (CALM3) calmodulin 1 pseudogene 1 (CALM1P1) Calmodulin-like 3 (CALML3) ... Calmodulin-like 4 (CALML4) Calmodulin-like 5 (CALML5) Calmodulin-like 6 (CALML6) Calmodulin belongs to one of the two main ... Calmodulin can also make use of the calcium stores in the endoplasmic reticulum, and the sarcoplasmic reticulum. Calmodulin can ... Calcium binding by calmodulin exhibits considerable cooperativity, making calmodulin an unusual example of a monomeric (single- ...
Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene. Calmodulin 1 is the archetype of the family of calcium- ... Calmodulin contains 148 amino acids and has 4 calcium-binding EF hand motifs. Its functions include roles in growth and the ... "Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)". Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y (Sep 2002 ... Calmodulin 1 has been shown to interact with: AKAP9, Androgen receptor, IQGAP1, PPEF1, and TRPV1. GRCh38: Ensembl release 89: ...
... Christine Hughes hughe014 at mc.duke.edu Sat Mar 4 13:09:33 EST 1995 *Previous message: ...
1986) Effect of Calmodulin Inhibitors on Thyroid Hormone Secretion. In: Medeiros-Neto G., Gaitan E. (eds) Frontiers in ... Myosin Light Chain Kinase Thyroid Lobe Calmodulin Inhibitor Thyroid Hormone Secretion Thyroid Hormone Release These keywords ... Chlorpromazine inhibits the action of calmodulin which is contained in the thyroid and may act on tubulin assembly-disassembly ... 3). These findings led us to postulate that calmodulin plays a role in TSH-induced thyroid hormone secretion. ...
Scanning the human proteome for calmodulin-binding proteins. Xinchun Shen, C. Alexander Valencia, Jack Szostak, Biao Dong, Rihe ... Scanning the human proteome for calmodulin-binding proteins. Xinchun Shen, C. Alexander Valencia, Jack Szostak, Biao Dong, Rihe ... Scanning the human proteome for calmodulin-binding proteins. Xinchun Shen, C. Alexander Valencia, Jack Szostak, Biao Dong, and ... Among a number of Ca2+ sensors in the eukaryotic cell, calmodulin (CaM) is the most widespread and the best studied. Employing ...
Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin.. Magnani R, Dirk ... Calmodulin N-methyltransferase. Partial purification and characterization.. Rowe PM, Wright LS, Siegel FL.. J. Biol. Chem. 261 ... Literature: Calmodulin-lysine N-methyltransferase (IPR025800). References used in this entry. The following publications were ...
Calcium-Calmodulin-Dependent Protein Kinase Type 2 delta Subunit. *Calcium Calmodulin Dependent Protein Kinase Type 2 delta ... Calcium-Calmodulin-Dependent Protein Kinase Type 2 alpha Subunit. *Calcium Calmodulin Dependent Protein Kinase Type 2 alpha ... Calcium-Calmodulin-Dependent Protein Kinase Type 2 beta Subunit. *Calcium Calmodulin Dependent Protein Kinase Type 2 beta ... Calcium-Calmodulin-Dependent Protein Kinase Type 2 gamma Subunit. *Calcium Calmodulin Dependent Protein Kinase Type 2 gamma ...
calmodulin-1. Names. Calmodulin 1 (phosphorylase kinase, delta). caM. calmodulin I. NP_114175.1. *EC 2.7.11.19 ... Calmodulin induced events, organism-specific biosystem (from REACTOME) Calmodulin induced events, organism-specific biosystem ... Title: Pivoting between calmodulin lobes triggered by calcium in the Kv7.2/calmodulin complex. ... Calm1 calmodulin 1 [Rattus norvegicus] Calm1 calmodulin 1 [Rattus norvegicus]. Gene ID:24242 ...
Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Meador, W.E., Means, A.R.,& ... Calmodulin. A. 148. Homo sapiens. Mutation(s): 0 Gene Names: CALM1, calm2, calm3, CALM, CAM, CAM1. ... Structure of Calmodulin Bound to the Hydrophobic IQ Domain of the Cardiac Ca(v)1.2 Calcium Channel.. Fallon, J.L., Halling, D.B ... We present the 1.45 A crystal structure of Ca2+-calmodulin bound to a 21 residue peptide corresponding to the IQ domain of Ca(v ...
Calmodulin. A. 76. Rattus norvegicus. Mutation(s): 0 Gene Names: Calm1, Calm, Cam, Cam1, CaMI. ... Calmodulin (CaM) is a 16.8-kDa calcium-binding protein involved in calcium-signal transduction. It is the canonical member of ... Calmodulin (CaM) is a 16.8-kDa calcium-binding protein involved in calcium-signal transduction. It is the canonical member of ... A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step.. Warren, J.T., Guo ...
Studies in a variety of model systems are beginning to identify components of the calcium/calmodulin cascade required for ... Calcium and its ubiquitous intracellular receptor calmodulin are required for cell proliferation. ... Two calcium/calmodulin-dependent enzymes, the multifunctional calcium/calmodulin-dependent protein kinase and the protein ... Studies in a variety of model systems are beginning to identify components of the calcium/calmodulin cascade required for ...
Calmodulin Point Mutations Affect Drosophila Development and Behavior. Heidi B. Nelson, Robert G. Heiman, Clare Bolduc, Gae E. ... Calmodulin Point Mutations Affect Drosophila Development and Behavior. Heidi B. Nelson, Robert G. Heiman, Clare Bolduc, Gae E. ... Calmodulin Point Mutations Affect Drosophila Development and Behavior. Heidi B. Nelson, Robert G. Heiman, Clare Bolduc, Gae E. ... Calmodulin Point Mutations Affect Drosophila Development and Behavior Message Subject (Your Name) has forwarded a page to you ...
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structure. Various spectroscopic ... Bending of the calmodulin central helix: a theoretical study.. *van der Spoel D ... The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structure. Various spectroscopic ...
C. D. DeMaria, T. W. Soong, B. A. Alseikhan, R. S. Alvania, D. T. Yue, Calmodulin bifurcates the local Ca2+ signal that ... The calcium-binding protein calmodulin (CaM) is thought to modulate the P/Q-type calcium channel of neurons in two ways: to ...
provide evidence that calmodulin (CaM) directly attenuates D2 receptor activation of the inhibitory G protein Gαi1. In the ... Bofill-Cardona, E., Kudlacek, O., Yang, Q., Ahorn, H., Freissmuth, M., and Nanoff, C. (2000) Binding of calmodulin to the D2- ...
It is a Ca 2+ /calmodulin-dependent, truncated monomer (1-325 amino acid residues) of the α subunit. Autophosphorylation of ... threonine 286 in the presence of Ca 2+ and calmodulin activates CaMKII and produces substantial Ca 2+ /calmodulin-independent ... Calmodulin-Dependent Protein Kinase II (CaMKII) is a serine/threonine kinase. ... Calmodulin-Dependent Protein Kinase II (CaMKII) is a serine/threonine kinase. It is a Ca2+/calmodulin-dependent, truncated ...
Rabbit polyclonal Calmodulin antibody validated for WB and tested in Human and Mouse. Immunogen corresponding to synthetic ... Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated ... All lanes : Anti-Calmodulin antibody (ab105498) at 1 µg/ml. Lane 1 : Ramos (Human Burkitts lymphoma cell line) Whole Cell ... Synthetic peptide conjugated to KLH derived from within residues 100 to the C-terminus of Human Calmodulin. Read Abcams ...
Methodology/Principal Findings We present studies of the photounbinding of labeled calmodulin (CaM) from a set of CaM-binding ...
Calmodulin The sequence for Calmodulin is shown below. Calmodulin, which mediates many calcium-driven metabolic reactions, is ... Calmodulin. Homo sapiens (human). ( ) = alpha helix [ ] = beta strand { } = turn Underlined: calcium binding site ... In calmodulin, each of the calcium-binding sites is flanked by or partly embedded in two long helices, with the Ca++ ion held ... Click to hear calmodulin alpha themes. Although the helical sequences of each reiteration of the theme are not as strongly ...
Calmodulin (CaM) senses local changes in Ca2+ concentration and relays the information to numerous interaction partners. The ... Calmodulin (CaM) senses local changes in Ca2+ concentration and relays the information to numerous interaction partners. The ... FIGURE 1. Human calmodulin mutations. (A) The calmodulin (CaM) protein has two lobes connected by a flexible α-helical linker. ... 2017). The arrhythmogenic calmodulin p.Phe142Leu mutation impairs C-domain Ca 2+ binding but not calmodulin-dependent ...
... binding protein calmodulin binds to and activates several cellular enzymes in response to a rise in Ca2+ concentration. It ... Calmodulin-binding domains: just two faced or multi-faceted? Trends Biochem Sci. 1995 Jan;20(1):38-42. doi: 10.1016/s0968-0004( ... The Ca(2+)-binding protein calmodulin binds to and activates several cellular enzymes in response to a rise in Ca2+ ...
Calmodulin can bind up to four calcium ions, and the three-dimensional spatial structure of calmodulin varies with the number ... So we can directly observe how the calmodulin snatches the amino acid chain and folds itself, to hold its target fast." ... A so-called signaling protein and "calcium sensor," calmodulin gives start and stop signals for a great number of intracellular ... Rief and Junker used mechanical force - actually pulling on complexes of calmodulin and the target peptides at rates of 1 ...
Calcium/calmodulin-stimulated cyclic nucleotide phosphodiesteraseImported. Automatic assertion inferred from database entriesi ... tr,Q16713,Q16713_HUMAN Calcium/calmodulin-stimulated cyclic nucleotide phosphodiesterase (Fragment) OS=Homo sapiens OX=9606 PE= ...
For single-step purification of calmodulin-binding peptide fusion proteins.Purification of calmodulin-regulated proteins from ... Calmodulin Sepharose 4B from GE Healthcare, formerly Amersham Biosciences,Calmodulin Sepharose 4B, 10 ml. ... Calmodulin Sepharose 4B, 10 ml. For single-step purification of calmodulin-binding peptide fusion proteins.Purification of ... Anti-CaMKII (Calmodulin-dependent Protein Kinase II) Monoclonal Antibody, Unconjugated, Clone 6G9 (2) from CHEMICON. 2. ...
Here, I report the cloning and sequencing of the third calmodulin cDNA (pRCM4) and two additional rat calmodulin genes. The ... original calmodulin gene is named CaM I (pRCM1) and t … ... of a rat calmodulin gene and two distinct rat calmodulin cDNAs ... The original calmodulin gene is named CaM I (pRCM1) and the newly discovered calmodulin genes are named CaM II (pRCM3) and CaM ... Elsewhere, we have reported the structure of a rat calmodulin gene and two distinct rat calmodulin cDNAs, pRCM1 and pRCM3. Here ...
The lollipop plot above illustrates recurrent (observed in 3 or more out of 4440 TCGA tumor samples from 15 cancer types) and therefore potentially oncogenic missense mutations (click on Show Cancer Mutations). The bar plot below shows the proportion of tumor samples that have any kind of altering mutation(s) in the given protein. ...
calmodulin, [Ca2+]i, intracellular Ca2+ concentration;. NINAC,. neither inactivation nor afterpotential protein;. ISOC,. store- ... Calmodulin regulation of light adaptation and store-operated dark current in Drosophila photoreceptors. Assaf Arnon, Boaz Cook ... Calmodulin Regulation of Ca2+ Release from Ryanodine-Sensitive Stores Is Essential for Light Excitation.. The LIC was rescued ... Calmodulin regulation of light adaptation and store-operated dark current in Drosophila photoreceptors ...
... Manabu Kubokawa, Kazuyoshi ... Roles of calcineurin (CaN), a Ca2+/calmodulin- (CaM-) dependent protein phosphatase, and Ca2+/CaM-dependent protein kinase-II ( ...
Purification of calmodulins and Cmd1p-Myo2p-binding assay. (A) Purification of wild-type and mutant calmodulins. Purified wild- ... In the cmd1-226 cells, polarized calmodulin localization was lost (Figure 3F). The loss of calmodulin localization is a ... Amino acid requirement at position Phe92 of calmodulin: In this study, we demonstrate that Phe92 of yeast calmodulin is ... 1986 Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47: 423-431. ...
  • Once bound to Ca2+, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases. (wikipedia.org)
  • Together, these features allow calmodulin to recognize some 300 target proteins exhibiting a variety of CaM-binding sequence motifs. (wikipedia.org)
  • Canonical" targets of calmodulin, such as myosin light-chain kinases and CaMKII, bind only to the Ca2+-bound protein, whereas some proteins, such as NaV channels and IQ-motif proteins, also bind to calmodulin in the absence of Ca2+. (wikipedia.org)
  • This influence of target binding on Ca2+ affinity is believed to allow for Ca2+ activation of proteins that are constitutively bound to calmodulin, such as small-conductance Ca2+-activated potassium (SK) channels. (wikipedia.org)
  • Many of the proteins that calmodulin binds are unable to bind calcium themselves, and use calmodulin as a calcium sensor and signal transducer. (wikipedia.org)
  • Calmodulin 1 is the archetype of the family of calcium-modulated (calmodulin) proteins of which nearly 20 members have been found. (wikipedia.org)
  • Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). (abcam.com)
  • It's well known that the protein calmodulin specifically targets and steers the activities of hundreds of other proteins - mostly kinases - in our cells, thus playing a role in physiologically important processes ranging from gene transcription to nerve growth and muscle contraction But just how it distinguishes between target proteins is not well understood. (innovations-report.com)
  • The results reveal new details of how calmodulin binds and regulates its target proteins. (innovations-report.com)
  • A so-called signaling protein and "calcium sensor," calmodulin gives start and stop signals for a great number of intracellular activities by binding and releasing other proteins. (innovations-report.com)
  • This structure in turn helps to determine which amino acid chains - peptides and proteins - the calmodulin will bind. (innovations-report.com)
  • For single-step purification of calmodulin-binding peptide fusion proteins.Purification of calmodulin-regulated proteins from all eukaryotic cells. (bio-medicine.org)
  • It seems likely that calmodulin performs diverse functions by interacting with many different target proteins. (genetics.org)
  • Indeed, a large number of calmodulin-binding proteins possessing diverse activities in vitro have been identified so far ( C ohen and K lee 1988 ). (genetics.org)
  • Many of these proteins have been well characterized biochemically, but it has generally remained unclear which calmodulin targets have functional significance and how these functions are regulated in the cell. (genetics.org)
  • The effect of Ca 2+ and calmodulin on phosphorylation of islet secretory granule proteins was studied. (diabetesjournals.org)
  • The addition of 2.4 μM calmodulin markedly enhanced the phosphorylation of the 58,000- and 48,000- M r proteins and resulted in the phosphorylation of a major protein whose molecular weight (64,000 M r ) is identical to that of one of the calmodulin binding proteins located on the granule surface. (diabetesjournals.org)
  • Among the intracellular proteins involved in Ca2+-signal deciphering, calmodulin (CaM) plays a pivotal role in controlling Ca2+-homeostasis and downstream Ca2+-based signalling events. (sigmaaldrich.com)
  • Calmodulin (CaM) pull-down assay is an effective way to investigate the interaction of CaM with various proteins. (jove.com)
  • The CaBP family shares much similarity with CaM I (calmodulin), and it has been shown that CaBP proteins can substitute functionally for, and possibly augment the function of, CaM I. CaBP7 (Calcium-binding protein 7), contains two EF-hand domains for calcium binding and shares 70% homology with CaBP8 and 50% homology with CaM I. It negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. (thermofisher.com)
  • Calmodulin (CaM) is a ubiquitous cytosolic Ca2+-binding protein able to bind and regulate hundreds of different proteins. (uwaterloo.ca)
  • Additionally we are shipping Calmodulin 1 Kits (47) and Calmodulin 1 Proteins (27) and many more products for this protein. (antibodies-online.com)
  • Multifunctional calcium-calmodulin-dependent protein kinase (CaM kinase) transduces transient elevations in intracellular calcium into changes in the phosphorylation state and activity of target proteins. (sciencemag.org)
  • As it binds calcium, calmodulin undergoes conformational changes which can increase its affinity for target proteins. (thermofisher.com)
  • A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. (harvard.edu)
  • Calmodulin undergoes a conformational change upon binding to calcium, which enables it to bind to specific proteins for a specific response. (acris-antibodies.com)
  • The distributions of two key proteins, PSD-95 and calcium/calmodulin-dependent protein kinase II (CaMKII), are compared. (jneurosci.org)
  • Of all the known members of the superfamily of proteins that utilize the EF-hand helix-loop-helix configuration to bind Ca ++ , calmodulin is unique. (springer.com)
  • In addition calmodulin serves as the obligatory Ca ++ -dependent activator of a variety of enzymes, exists in enzyme and organelle complexes in the Ca free state and is associated with several intracellular structural proteins. (springer.com)
  • When the intracellular calcium level rises to 10-5 M, four Ca2+ ions bind to calmodulin, and this Ca2+-calmodulin complex binds the target proteins, initiating various signaling cascades. (agscientific.com)
  • In Alzheimer's disease (AD), irregular calcium homeostasis seems to trigger CaM and its binding proteins, to enhance plaque formation and neurofibrillary degeneration, which results in cell death.In Parkinson's disease (PD), Calmodulin has been found to interact, in a calcium-dependent manner, with Alpha-Synuclein, which is associated with the progression of PD. (agscientific.com)
  • article{df0fc3a3-37f5-4e45-a3b0-1ef7b12608e6, abstract = {The aim of this study was to investigate the involvement of calmodulin in phospholipase D activation in SH-SY5Y cells. (lu.se)
  • The Ca(2+)-binding protein calmodulin binds to and activates several cellular enzymes in response to a rise in Ca2+ concentration. (nih.gov)
  • DCVJ binds to bovine brain calmodulin and emits strong fluorescence. (sigmaaldrich.com)
  • Equilibrium fluorescence spectroscopy experiments indicate that Ca²⁺/calmodulin binds GluN2A with high affinity (5.2 ± 2.4 nM) in vitro. (oregonstate.edu)
  • Calmodulin can undergo post-translational modifications, such as phosphorylation, acetylation, methylation and proteolytic cleavage, each of which has potential to modulate its actions. (wikipedia.org)
  • Phosphorylation of calmodulin. (wikipedia.org)
  • Calmodulin had no effect on phosphorylation in the absence of Ca 2+ but was effective in the presence of calcium between 10 nM and 50 μM. (diabetesjournals.org)
  • Calcium/calmodulin-dependent protein kinase II regulates the phosphorylation of CREB in NMDA-induced retinal neurotoxicity," Brain Research , vol. 1184, no. 1, pp. 306-315, 2007. (hindawi.com)
  • These Pb2+-induced changes in CaMKII activity could not be explained by changes in enzyme phosphorylation at threonine-286 or sensitivity to calmodulin. (cdc.gov)
  • The increased rd1 phosducin phosphorylation coincided with increased activation of calcium/calmodulin-activated protein kinase II, which is known to utilize phosducin as a substrate. (mcponline.org)
  • Contractile function was also preserved in colon ascendens stent peritonitis myocytes isolated from transgenic mice expressing a calcium and calmodulin-dependent protein kinase II inhibitory peptide (AC3-I) and in colon ascendens stent peritonitis myocytes isolated from mutant mice that have the ryanodine receptor 2 calcium and calmodulin-dependent protein kinase II-dependent phosphorylation site (serine 2814) mutated to alanine (S2814A). (ovid.com)
  • Calcium and calmodulin-dependent protein kinase II, through phosphorylation of the ryanodine receptor would lead to Ca 2+ leak from the sarcoplasmic reticulum, reducing sarcoplasmic reticulum Ca 2+ content, Ca 2+ transient amplitude and contractility. (ovid.com)
  • Cyclic AMP-dependent phosphorylation of the 22-kDa polypeptide was inhibited by the protein kinase inhibitor and calmodulin-dependent phosphorylation was inhibited by chlorpromazine and EGTA. (eurekamag.com)
  • Calmodulin, which mediates many calcium-driven metabolic reactions, is found in all eukaryotes and its sequence is remarkably conserved. (whozoo.org)
  • Calmodulin (CaM) is a Ca 2+ sensor and mediates Ca 2+ signaling through binding of numerous target ligands. (rsc.org)
  • A gene on chromosome 17p13.2 that encodes a calcium/calmodulin-dependent serine/threonine protein kinase, which mediates many of calcium's second messenger effects. (thefreedictionary.com)
  • Calmodulin-Dependent Protein Kinase II (CaMKII) is a serine/threonine kinase. (neb.com)
  • Autophosphorylation of threonine 286 in the presence of Ca 2+ and calmodulin activates CaMKII and produces substantial Ca 2+ /calmodulin-independent activity (1,2). (neb.com)
  • Roles of calcineurin (CaN), a Ca 2+ /calmodulin- (CaM-) dependent protein phosphatase, and Ca 2+ /CaM-dependent protein kinase-II (CaMKII) in modulating K + channel activity and the intracellular Ca 2+ concentration ([Ca 2+ ] i ) have been investigated in renal tubule epithelial cells. (hindawi.com)
  • In the present study, we examined whether calcium/calmodulin-dependent protein kinase II (CaMKII) is affected by chronic developmental Pb2+ exposure. (cdc.gov)
  • Functional plasticity of neuronal gap junctions involves the interaction of the neuronal connexin36 with calcium/calmodulin-dependent kinase II (CaMKII). (frontiersin.org)
  • The important relationship between Cx36 and CaMKII must also be considered in the context of another protein partner, Ca 2+ loaded calmodulin, binding an overlapping site in the carboxy-terminus of Cx36. (frontiersin.org)
  • involves interaction of Cx36 with the calcium/calmodulin-dependent kinase II (CaMKII). (frontiersin.org)
  • In this paper we use the FBAR to measure the binding of calcium and the CaMKII peptide to calmodulin. (mdpi.com)
  • We determined the positions of calcium/calmodulin-dependent protein kinase II (CaMKII) and PSD-95 within the three-dimensional structure of isolated PSDs using immunogold labeling, rotary shadowing, and electron microscopic tomography. (jneurosci.org)
  • The multifunctional calcium/calmodulin-dependent protein kinase II (CaMKII) is activated by catecholamines and angiotensin II, and CaMKII inhibition prevents isoproterenol- and angiotensin II-mediated cardiomyopathy. (ahajournals.org)
  • In this review, the functions of multifunctional Ca2+/calmodulin-dependent protein kinase II (CaMKII) in VSM phenotype switching and synthetic phenotype function are considered. (ovid.com)
  • A cultured macaque choroid-retinal endothelial cell line (RF/6A) was incubated in normal glucose (NG), NG plus the Ca 2+ entry blocker 2-aminoethoxydiphenyl borate (2-APB), high glucose (HG), or HG plus either 2-APB, the c-jun N-terminal kinase (JNK) inhibitor SP600125, or the calcium/calmodulin-dependent protein kinase II (CaMKII) inhibitor KN93. (molvis.org)
  • CaMKII (Calcium/calmodulin-dependent protein kinase II) is a ubiquitous serine/threonine protein kinase that is abundant in the brain as a major constituent of the postsynaptic density (PSD). (neuromics.com)
  • Calcium/calmodulin-dependent protein kinase II activity and expression are altered in the hippocampus of Pb2+- exposed rats. (cdc.gov)
  • Okamoto H., Ichikawa K. (1997) Autophosphorylation Versus Dephosphorylation of Ca 2+ /Calmodulin-Dependent Protein Kinase II. (springer.com)
  • Colon ascendens stent peritonitis hearts showed a significant increase in oxidation-dependent calcium and calmodulin-dependent protein kinase II activity, which could be prevented by pretreating animals with the antioxidant tempol. (ovid.com)
  • Pharmacologic inhibition of calcium and calmodulin-dependent protein kinase II with 2.5 µM of KN93 prevented the decrease in cell shortening, Ca 2+ transient amplitude, and sarcoplasmic reticulum Ca 2+ content in colon ascendens stent peritonitis myocytes. (ovid.com)
  • Results indicate that oxidation and subsequent activation of calcium and calmodulin-dependent protein kinase II has a causal role in the contractile dysfunction associated with sepsis. (ovid.com)
  • Development of organ-specific calcium and calmodulin-dependent protein kinase II inhibitors may result in a beneficial therapeutic strategy to ameliorate contractile dysfunction associated with sepsis. (ovid.com)
  • Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. (wikipedia.org)
  • A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. (nih.gov)
  • Nghiem P, Saati SM, Martens CL, Gardner P, Schulman H: Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. (hmdb.ca)
  • We assess the ability of 2D-IR spectroscopy in combination with multivariate data analysis to quantify changes in secondary structure of the multifunctional calcium-binding messenger protein Calmodulin (CaM) as a function of temperature and Ca2+ concentration. (strath.ac.uk)
  • Your search returned 54 calmodulin 3 (phosphorylase kinase, delta) ELISA ELISA Kit across 1 supplier. (biocompare.com)
  • Furthermore, target binding alters the binding affinity of calmodulin toward Ca2+ ions, which allows for complex allosteric interplay between Ca2+ and target binding interactions. (wikipedia.org)
  • Title: Oxidation of ryanodine receptor (RyR) and calmodulin enhance Ca release and pathologically alter, RyR structure and calmodulin affinity. (nih.gov)
  • Gel overlay assay shows that a mutant calmodulin with the F92A alteration has severely reduced binding affinity to a GST-Myo2p fusion protein. (genetics.org)
  • By fluorescence emission anisotropy, the affinity of CaM kinase for dansylated calmodulin was measured and found to increase 1000 times after autophosphorylation of the threonine at position 286 of the protein. (sciencemag.org)
  • Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene. (wikipedia.org)
  • On www.antibodies-online.com are 253 Calmodulin 1 (Calm1) Antibodies from 23 different suppliers available. (antibodies-online.com)
  • Both FMRP deficiency in Fmr1 (I304N) mice and Fmr1 knockdown impeded the axonal delivery of miR -181d, Map1b , and Calm1 and reduced the protein levels of MAP1B and calmodulin in axons. (antibodies-online.com)
  • Strehler, E. E. : Localization of the human bona fide calmodulin genes CALM1, CALM2, and CALM3 to chromosomes 14q24-q31, 2p21.1-p21.3, and 19q13.2-q13.3. (acris-antibodies.com)
  • Recent genetic studies identified mutations in CALM1 or CALM2 , 2 of the 3 human genes encoding calmodulin (CaM), in both catecholaminergic polymorphic ventricular tachycardia (CPVT) and long QT syndrome (LQTS). (ahajournals.org)
  • One of four intragenic complementing groups of temperature-sensitive yeast calmodulin mutations, cmd1A , results in a characteristic functional defect in actin organization. (genetics.org)
  • We previously succeeded in systematic isolation of 14 temperature-sensitive calmodulin mutations by phenylalanine-to-alanine mutagenesis ( O hya and B otstein 1994b ). (genetics.org)
  • The most striking finding from systematic mutagenesis of calmodulin was that the mutations formed four intragenic complementation groups ( O hya and B otstein 1994a ). (genetics.org)
  • Thus, each complementation group of calmodulin mutations can be thought of as producing a functional defect by loss of interaction with different essential target ligands. (genetics.org)
  • Here, I report the cloning and sequencing of the third calmodulin cDNA (pRCM4) and two additional rat calmodulin genes. (nih.gov)
  • The original calmodulin gene is named CaM I (pRCM1) and the newly discovered calmodulin genes are named CaM II (pRCM3) and CaM III (pRCM4). (nih.gov)
  • In all calmodulin genes, the first intron separates the initiation codon (ATG) from the coding region of the protein. (nih.gov)
  • Here, we show that two CALMODULIN-LIKE genes, CML46 and CML47 , negatively regulate salicylic acid accumulation and immunity in Arabidopsis ( Arabidopsis thaliana ). (plantphysiol.org)
  • Induction of TLR4-target genes entails calcium/calmodulin-dependent regulation of chromatin remodeling. (diva-portal.org)
  • Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. (abcam.com)
  • Several calmodulin-dependent enzymes, including protein kinases and protein phosphatases, have been studied in yeast. (genetics.org)
  • Calmodulin (CaM) is a ubiquitous calcium-binding protein responsible for the binding and activation of a vast number of enzymes and signaling pathways. (uwaterloo.ca)
  • Calmodulin-dependent phosphodiesterase (CaMPDE) is one of the key enzymes involved in the complex interactions which occur between the cyclic-nucleotide and Ca2+ second-messenger systems. (biochemj.org)
  • Indeed some calmodulin-dependent enzymes are more widely distributed among phyla and between cell types of a given organism than are the other members of the calmodulin superfamily 2 . (springer.com)
  • The ubiquitous Ca2+-regulatory protein calmodulin activates target enzymes as a response to submicromolar Ca2+ increases in a background of millimolar Mg2+. (ruc.dk)
  • Calmodulin is a small thermostable protein which has been involved in the regulation of a number of cellular activities such as cyclic nucleotide and glycogen metabolism, smooth muscle contraction, intracellular motility, and calcium transport. (springer.com)
  • Kurosaki, F. , Kaburaki, H. , Nishi, A. 1994 Involvement of plasma membrane-located calmodulin in the response decay of cyclic nucleotide-gated cation channel of cultured carrot cells. (wiley.com)
  • E114A and L116T activated cyclic nucleotide phosphodiesterase (PDE) and NAD + kinase (NADK) similar to wild-type calmodulin, but lost their ability to be methylated. (portlandpress.com)
  • CALMODULIN, a highly conserved calcium-binding protein, has been implicated in Ca 2+ -mediated signaling cascades, including muscle contraction and neurotransmitter release ( C ohen and K lee 1988 ). (genetics.org)
  • Calmodulin is a small, highly conserved calcium binding protein found in all eukaryotic cells. (thermofisher.com)
  • The following product was used in this experiment: Calmodulin 3 Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-70445, RRID AB_2691194. (thermofisher.com)
  • AM03186PU-N Calmodulin antibody staining of Formalin-Fixed, Paraffin-Embedded Human Brain, Cerebellum at 10 µg/ml after heat-induced antigen retrieval. (acris-antibodies.com)
  • Cell lysates of NIH3T3 (50 µg) were resolved by SDS-PAGE, transferred to NC membrane and probed with anti-Human Calmodulin Antibody AM03186PU-N (1/500). (acris-antibodies.com)
  • It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of calmodulin. (wikipedia.org)
  • Calmodulin (CAM) is recognized as a major intermediary in intracellular calcium signaling, but as yet little is known of its role in developmental and behavioral processes. (genetics.org)
  • Studies have found that calmodulin participates in the regulation of several biological processes including energy and biosynthetic metabolism, cell motility, exocytosis, cytoskeletal assembly, and intracellular modulation of both cAMP and calcium concentrations. (thermofisher.com)
  • Calmodulin (CaM) is an intracellular calcium receptor found ubiquitously in eukaryotes. (agscientific.com)
  • Activation of the enzyme is ligand-dependent-peptides with higher affinities for wild-type calmodulin exhibit increased switch activity. (harvard.edu)
  • However, CaM EKL retained the ability to bind to NADK and inhibited activation by wild-type calmodulin. (portlandpress.com)
  • Over the same Ca2+ range, a decrease in molecular ellipticity at 222 nm and an increase in tyrosine fluorescence of calmodulin were observed. (sigmaaldrich.com)
  • Calmodulin trapping provides for molecular potentiation of calcium transients and may enable detection of their frequency. (sciencemag.org)
  • To identify the molecular processes leading to these adaptations, we performed Cre/loxP-mediated genetic ablations of two key regulators of gene expression in response to activity, the Ca2+/calmodulin-dependent protein kinase IV (CaMKIV) and its postulated main target, the cAMP-responsive element binding protein (CREB). (kb.se)
  • Calmodulin-dependent phosphodiesterase exists in different isoenzymic forms, which exhibit distinct molecular and/or catalytic properties. (biochemj.org)
  • 2001), Molecular basis of calmodulin tethering and Ca2. (xenbase.org)
  • Molecular basis of calmodulin tethering and Ca2+-dependent inactivation of L-type Ca2+ channels. (xenbase.org)
  • Rief and Junker used mechanical force - actually pulling on complexes of calmodulin and the target peptides at rates of 1 nanometer per second or less - to slow down the processes to observable time scales and to clearly separate the individual unbinding steps. (innovations-report.com)
  • Furthermore, Ca 2+ loaded calmodulin activates Cx36 channels, which is different to other connexins. (frontiersin.org)
  • In this system, we investigate the hitherto unknown physiological roles of calmodulin (CaM) in light adaptation and in regulation of the inward current that is brought about by depletion of cellular Ca 2+ stores. (pnas.org)
  • The regulation of nitric oxide synthase (NOS) by calmodulin (CaM) plays a major role in a number of key physiological and pathological processes. (uwaterloo.ca)
  • Data suggest that Cys3602 in RyR2 (ryanodine receptor 2 (show RYR2 Antibodies )) plays important role in activation/termination of Ca2 (show CA2 Antibodies )+ release, but it is not essential for calmodulin regulation of RyR2 (show RYR2 Antibodies ). (antibodies-online.com)
  • These observations are consistent with the notion that differential regulation by calmodulin and Ca2+ is an important function of these isoenzymes, which provide fine-tuning mechanisms for calmodulin action. (biochemj.org)
  • Calmodulin antagonists may be useful tools to further elucidate the mechanisms of phospholipase D regulation. (lu.se)
  • Overexpression of CaM 1234 (calmodulin mutant lacking 4 Ca 2+ binding sites) strongly suppressed the effects of l μM Ca 2+ i on Ca v 3.3, implying that CaM is involved in the Ca 2+ i regulation effects on Ca v 3.3. (aspetjournals.org)
  • The flexible central domain of calmodulin allows the protein to wrap around its target, although alternate modes of binding are known. (wikipedia.org)
  • The interdependence of Ca2+ and Mg2+ binding in the N-terminal domain of calmodulin was therefore studied using 43Ca NMR, 1H-15N NMR, and fluorescent Ca2+ chelator techniques. (ruc.dk)
  • Title: Polarized axonal surface expression of neuronal KCNQ potassium channels is regulated by calmodulin interaction with KCNQ2 subunit. (nih.gov)
  • Ca2+-dependent inactivation (CDI) and facilitation (CDF) of the Ca(v)1.2 Ca2+ channel require calmodulin binding to a putative IQ motif in the carboxy-terminal tail of the pore-forming subunit. (rcsb.org)
  • It is a Ca 2+ /calmodulin-dependent, truncated monomer (1-325 amino acid residues) of the α subunit. (neb.com)
  • As the Ca 2+ -sensor for Ca 2+ -dependent inactivation, calmodulin (CaM) has been proposed, but never definitively demonstrated, to be a constitutive Ca V 1.2 Ca 2+ channel subunit. (jneurosci.org)
  • The bovine lung CaMPDE isoenzyme contains calmodulin as a tightly bound subunit, so that a change in calmodulin concentration had no effect on the [Ca2+]-dependence of activation of this isoenzyme. (biochemj.org)
  • In addition, concerted stimulation of Ca2+-ATPase by exogenous calmodulin and added catalytic subunit of cAMP-dependent protein kinase was observed. (eurekamag.com)
  • Calmodulin (CaM) senses local changes in Ca 2+ concentration and relays the information to numerous interaction partners. (frontiersin.org)
  • Random replacement and site-directed mutagenesis at position 92 of calmodulin indicate that hydrophobic and aromatic residues are allowed at this position, suggesting an importance of hydrophobic interaction between calmodulin and Myo2p. (genetics.org)
  • Direct interaction of Ca²⁺/calmodulin with GluN2A was not affected by disruption of classic sequence motifs associated with Ca²⁺/calmodulin target recognition, but was critically dependent upon Trp-1014. (oregonstate.edu)
  • Synthetic peptide conjugated to KLH derived from within residues 100 to the C-terminus of Human Calmodulin. (abcam.com)
  • The association of calcium-bound calmodulin (CaM ) with DREAM is mediated by a short amphipathic amino acid sequence located between residues 29 and 44 on DREAM. (antibodies-online.com)
  • Calcium fingerprints induced by calmodulin interactors in eukaryotic cells. (sigmaaldrich.com)
  • Calmodulin, calcium-modulated protein, is a calcium-binding protein expressed in all eukaryotic cells. (acris-antibodies.com)
  • These experiments demonstrate the existence of a new state in which calmodulin is bound to CaM kinase even though the concentration of calcium is basal. (sciencemag.org)
  • The measured frequency shift during the calcium adsorptions was found to be strongly dependent on the surface concentration of the immobilized calmodulin, which indicates that the measured signal is significantly influenced by the amount of water inside the calmodulin layer. (mdpi.com)
  • At identical concentrations of calmodulin, the bovine heart CaMPDE isoenzyme is stimulated at a much lower Ca2+ concentration than the bovine brain or lung isoenzymes. (biochemj.org)
  • Detects endogenous levels of Calmodulin only when phosphorylated at threonine 79 and serine 81. (abcam.com)
  • CAMK1D encodes a member of the Ca2+/calmodulin-dependent protein kinase 1 subfamily of serine/threonine kinases. (antikoerper-online.de)
  • Calcium/calmodulin-dependent protein kinase IV (CaMK4), a serine/threonine kinase expressed in T cells ( 6 ), regulates the activity of several transcription factors including CREM ( 7 ). (jimmunol.org)
  • CAMK4 belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. (antikoerper-online.de)
  • Moreover, the predominantly hydrophobic nature of binding between calmodulin and most of its targets allows for recognition of a broad range of target protein sequences. (wikipedia.org)
  • This structure shows that parallel binding of calmodulin to the IQ domain is governed by hydrophobic interactions. (rcsb.org)
  • Synthetic peptide corresponding to Human Calmodulin. (abcam.com)
  • A synthesized peptide derived from human Calmodulin, corresponding to a region within the internal amino acids. (thermofisher.com)
  • Yokokura, Yurimoto, Matsuoka, Imataki, Dobashi, Bandoh, Matsunaga: Calmodulin antagonists induce cell cycle arrest and apoptosis in vitro and inhibit tumor growth in vivo in human multiple myeloma. (antibodies-online.com)
  • In conclusion, our data indicate that calmodulin antagonists induce phospholipase D activity in SH-SY5Y cells via a tyrosine kinase dependent pathway. (lu.se)
  • The calcium-binding protein calmodulin (CaM) is thought to modulate the P/Q-type calcium channel of neurons in two ways: to facilitate and then to inhibit channel opening. (sciencemag.org)
  • Reduced calmodulin expression accelerates transient outward potassium current inactivation in diabetic rat heart. (nih.gov)
  • Calmodulin (CaM)-mediated Ca 2+ -induced inactivation is an ion channel regulatory mechanism that protects cells against the toxic effects of Ca 2+ overload. (sciencemag.org)
  • In many cases, Ca 2+ -induced inactivation directly uses the universal calcium sensor calmodulin (CaM) ( 9 ), but the structural mechanisms of CaM-dependent Ca 2+ -induced inactivation remain largely unknown. (sciencemag.org)
  • Calmodulin can bind up to four calcium ions, and the three-dimensional spatial structure of calmodulin varies with the number of calcium ions bound to it. (innovations-report.com)
  • Calmodulin can also bind to edema factor toxin from the anthrax bacteria. (acris-antibodies.com)
  • Calmodulin (CaM) is a second messenger protein that has evolved to bind tightly to a variety of targets and, as such, exhibits low binding specificity. (caltech.edu)
  • These results indicate that Ca 2+ -calmodulin-dependent protein kinases and endogenous substrates are present in islet secretory granules. (diabetesjournals.org)
  • We have reexamined the effects of added cAMP-dependent protein kinase and endogenous calmodulin-dependent kinase on Ca2+ transport in purified internal membranes from human platelets. (eurekamag.com)
  • F92A) is synthetically lethal with a mutation in MYO2 that encodes a class V unconventional myosin with calmodulin-binding domains. (genetics.org)
  • The Medicago truncatula DMI3 gene encodes a calcium- and calmodulin-dependent protein kinase (CCaMK) that is necessary for the establishment of both rhizobial and mycorrhizal symbioses. (apsnet.org)
  • Binding of calmodulin induces conformational rearrangements in the target protein via "mutually induced fit", leading to changes in the target protein's function. (wikipedia.org)
  • These results mean that the conformational change of calmodulin due to the Ca2+ binding induces the microenvironmental change of the DCVJ binding site from the flexible to the rigid state, resulting in inhibition of the intramolecular rotation of DCVJ and an increase in its fluorescence. (sigmaaldrich.com)
  • Ca(2 +) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail. (antibodies-online.com)
  • Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin. (ebi.ac.uk)
  • Calmodulin N-methyltransferase. (ebi.ac.uk)
  • We offer calmodulin-lysine N-methyltransferase Lysates for use in common research applications: Western Blot. (novusbio.com)
  • Each calmodulin-lysine N-methyltransferase Lysate is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • Our calmodulin-lysine N-methyltransferase Lysates can be used in a variety of model species. (novusbio.com)
  • Choose from our calmodulin-lysine N-methyltransferase Lysates. (novusbio.com)
  • Calmodulin N-methyltransferase (CaM KMT) is an evolutionarily conserved enzyme in eukaryotes that transfers three methyl groups to a highly conserved lysyl residue at position 115 in calmodulin (CaM). (unl.edu)
  • Calmodulin is trimethylated by a specific methyltransferase on Lys 115 , a residue located in a six amino acid loop (LGEKLT) between EF hands III and IV. (portlandpress.com)
  • The CDI sensor is thought to be calmodulin (CaM), the prototypical CaBP. (jneurosci.org)
  • Ca(2+)-insensitive forms of calmodulin (CaM) act as dominant negatives to prevent CDI, suggesting that CaM acts as a resident Ca(2+) sensor. (xenbase.org)
  • Methods developed by biophysicists at the Technische Universitaet Muenchen (TUM) have enabled them to manipulate and observe calmodulin in action, on the single-molecule scale. (innovations-report.com)
  • Professor Matthias Rief and colleagues at the Technische Universitaet Muenchen had previously shown that they could fix a single calmodulin molecule between a surface and the cantilever tip of a specially built atomic-force microscope, expose it to calcium ions in solution, induce peptide binding and unbinding, and measure changes in the molecule's mechanical properties as it did its work. (innovations-report.com)
  • Measuring the force needed to bend the calmodulin molecule out of its stable condition at any given moment enables the researchers to compute the energies associated with binding both the calcium ions and the amino acid chains. (innovations-report.com)
  • Original paper: "Single-molecule force spectroscopy distinguishes target binding modes of calmodulin," by Jan Philipp Junker and Matthias Rief, published in the online Early Edition of PNAS, Proceedings of the National Academy of Sciences for the week of August 10, 2009. (innovations-report.com)
  • Small molecule inhibitors of the human sirtuins and calmodulin-dependent protein kinases have shown promising anti-cancer activity in cell-based screens and animal models. (washington.edu)
  • We have synthesized analogues of these compounds, identifying more selective sirtuin inhibitors and more potent calmodulin-dependent protein kinase inhibitors.The sirtuins are a family of NAD+-dependent deacetylases that regulate cellular aging and gene silencing in simple organisms and appear to play important regulatory roles in human cells that make them attractive anti-cancer targets. (washington.edu)
  • Calmodulin is structurally quite similar to troponin C, another Ca2+-binding protein containing four EF-hand motifs. (wikipedia.org)
  • Calmodulin contains 148 amino acids and has 4 calcium-binding EF hand motifs. (wikipedia.org)
  • the protein's primary structure contains a nuclear localization signal, two DNA-binding domains (CG-1 and TIG), calmodulin binding motifs (IQ motifs) and ankyrin domains that may mediate protein-protein interactions. (atlasgeneticsoncology.org)
  • By applying mechanical force," Junker says, "we are able to dismantle the calmodulin-target peptide complex with surgical precision. (innovations-report.com)
  • It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE. (nih.gov)
  • Activity-dependent modulation of endocytosis by calmodulin at a large central synapse. (nih.gov)
  • Trifluoperazine and calmidazolium, calmodulin antagonists, produced a dose-dependent inhibition of the calmodulin effect. (diabetesjournals.org)
  • The adenosine 3',5'-monophosphate (cAMP) response element-binding protein (CREB) was shown to function as a Ca(2+)-regulated transcription factor and as a substrate for depolarization-activated Ca(2+)-calmodulin-dependent protein kinases (CaM kinases) I and II. (sciencemag.org)
  • Using mass spectrometry this study identified calmodulin as a calcium-dependent GluN2A (show GRIN2A Antibodies ) binding partner. (antibodies-online.com)
  • In this approach, calmodulin acts as the input domain, whose ligand-dependent conformational changes control the activity of the β-lactamase output domain. (harvard.edu)
  • Calcium-Calmodulin-Dependent Protein Kinases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • This graph shows the total number of publications written about "Calcium-Calmodulin-Dependent Protein Kinases" by people in Harvard Catalyst Profiles by year, and whether "Calcium-Calmodulin-Dependent Protein Kinases" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Calcium-Calmodulin-Dependent Protein Kinases" by people in Profiles. (harvard.edu)
  • Zusätzlich bieten wir Ihnen Calcium/calmodulin-Dependent Protein Kinase ID Proteine (13) und Calcium/calmodulin-Dependent Protein Kinase ID Kits (2) und viele weitere Produktgruppen zu diesem Protein an. (antikoerper-online.de)
  • In this study, we examined the role of the Ca 2+ /calmodulin (CaM)-dependent protein kinase (CaM-K) cascade in transcriptional activation of insulin. (diabetesjournals.org)
  • This effect of calcium is completely blocked by exposure to a Ca 2+ /calmodulin (CaM)-dependent protein kinase (CaM-K) inhibitor ( 10 ) and thus suggests that the actions of calcium on the insulin gene are mediated in part by Ca 2+ /CaM-Ks. (diabetesjournals.org)
  • Using insights from a co-crystal structure of a 3,5-bis(arylamino)-4 H -1,2,6-thiadiazin-4-one bound to calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2), several analogues were identified with micromolar activity through targeted displacement of bound water molecules in the active site. (mdpi.com)
  • a second event, dependent on calcium/calmodulin (CaM), is additionally required. (diva-portal.org)
  • The Ca2+ stimulation of the enzyme activity was calmodulin-dependent. (biochemj.org)
  • The enzyme had two pH optima (pH 7.4 and 9.0) and at both the activity was Ca2+-calmodulin-dependent. (biochemj.org)
  • The calmodulin antagonists, calmidazolium and trifluoperazine, induced an extensive increase in phosphatidylethanol formation, and thus increased basal phospholipase D activity, in a dose- and time-dependent manner. (lu.se)
  • However this breadth may also be related to calmodulin since calcineurin is the only known Ca /calmodulin-dependent protein phosphatase. (springer.com)
  • The activity of calcium/calmodulin-dependent protein kinase IV (CaMK4) is increased in T cells from patients with systemic lupus erythematosus (SLE) and has been shown to reduce IL-2 production by promoting the effect of the transcriptional repressor cAMP responsive element modulator-α on the IL2 promoter. (jimmunol.org)
  • SIRT2 appears to be the relevant target for cambinol-induced Daudi cell toxicity.KN-62, an inhibitor of the calmodulin-dependent protein kinases (CaMKs), enhances the terminal differentiation of retinoic acid sensitive human myeloid leukemia cell lines. (washington.edu)
  • Using mass spectrometry we identified calmodulin as a calcium-dependent GluN2A binding partner. (oregonstate.edu)
  • A 22-kDa protein was phosphorylated by both cAMP-dependent and calmodulin-dependent kinases at the same rate as stimulation of the Ca2+-ATPase. (eurekamag.com)
  • So we can directly observe how the calmodulin snatches the amino acid chain and folds itself, to hold its target fast. (innovations-report.com)
  • Calmodulin purified from the normal brain and gliomas of patients undergoing resection was identical to each other and to calmodulin prepared from rat cerebrum and glioma These characteristics included elution from a TSK phenyl high pressure liquid chromatography column, migration on 16% sodium dodecyl sulfate gels, amino acid composition, and inhibition by drugs. (aacrjournals.org)