A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A subtypes to distinct subcellular sites. They play a role in focusing the PROTEIN KINASE A activity toward relevant substrates. Over fifty members of this family exist, most of which bind specifically to regulatory subunits of CYCLIC AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA.
A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a lower affinity for cAMP than the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIALPHA SUBUNIT. Binding of this subunit by A KINASE ANCHOR PROTEINS may play a role in the cellular localization of type II protein kinase A.
A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a higher affinity for cAMP than that of the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIBETA SUBUNIT. Binding of this subunit by A KINASE ANCHOR PROTEINS may play a role in the cellular localization of type II protein kinase A.
A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
Transport proteins that carry specific substances in the blood or across cell membranes.
A cyclic AMP-dependent protein kinase subtype primarily found in particulate subcellular fractions. They are tetrameric proteins that contain two catalytic subunits and two type II-specific regulatory subunits.
A subclass of alpha-amylase ISOENZYMES that are secreted into SALIVA.
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.
Proteins found in SEMEN. Major seminal plasma proteins are secretory proteins from the male sex accessory glands, such as the SEMINAL VESICLES and the PROSTATE. They include the seminal vesicle-specific antigen, an ejaculate clotting protein; and the PROSTATE-SPECIFIC ANTIGEN, a protease and an esterase.
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.
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
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.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
The repeating contractile units of the MYOFIBRIL, delimited by Z bands along its length.
A form of CARDIAC MUSCLE disease, characterized by left and/or right ventricular hypertrophy (HYPERTROPHY, LEFT VENTRICULAR; HYPERTROPHY, RIGHT VENTRICULAR), frequent asymmetrical involvement of the HEART SEPTUM, and normal or reduced left ventricular volume. Risk factors include HYPERTENSION; AORTIC STENOSIS; and gene MUTATION; (FAMILIAL HYPERTROPHIC CARDIOMYOPATHY).
Myosin type II isoforms found in cardiac muscle.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
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.
Marked depression appearing in the involution period and characterized by hallucinations, delusions, paranoia, and agitation.
Pain in the breast generally classified as cyclical (associated with menstrual periods), or noncyclical, i.e. originating from the breast or nearby muscles or joints, ranging from minor discomfort to severely incapacitating.
SESQUITERPENES cyclized to one 10-carbon ring.
A physical property showing different values in relation to the direction in or along which the measurement is made. The physical property may be with regard to thermal or electric conductivity or light refraction. In crystallography, it describes crystals whose index of refraction varies with the direction of the incident light. It is also called acolotropy and colotropy. The opposite of anisotropy is isotropy wherein the same values characterize the object when measured along axes in all directions.
A class of nerve fibers as defined by their structure, specifically the nerve sheath arrangement. The AXONS of the myelinated nerve fibers are completely encased in a MYELIN SHEATH. They are fibers of relatively large and varied diameters. Their NEURAL CONDUCTION rates are faster than those of the unmyelinated nerve fibers (NERVE FIBERS, UNMYELINATED). Myelinated nerve fibers are present in somatic and autonomic nerves.
The use of diffusion ANISOTROPY data from diffusion magnetic resonance imaging results to construct images based on the direction of the faster diffusing molecules.
Any of various diseases affecting the white matter of the central nervous system.

The type and the localization of cAMP-dependent protein kinase regulate transmission of cAMP signals to the nucleus in cortical and cerebellar granule cells. (1/496)

cAMP signals are received and transmitted by multiple isoforms of cAMP-dependent protein kinases, typically determined by their specific regulatory subunits. In the brain the major regulatory isoform RIIbeta and the RII-anchor protein, AKAP150 (rat) or 75 (bovine), are differentially expressed. Cortical neurons express RIIbeta and AKAP75; conversely, granule cerebellar cells express predominantly RIalpha and RIIalpha. Cortical neurons accumulate PKA catalytic subunit and phosphorylated cAMP responsive element binding protein very efficiently into nuclei upon cAMP induction, whereas granule cerebellar cells fail to do so. Down-regulation of RIIbeta synthesis by antisense oligonucleotides inhibited cAMP-induced nuclear signaling in cortical neurons. Expression in cerebellar granule cells of RIIbeta and AKAP75 genes by microinjection of specific expression vectors, markedly stimulated cAMP-induced transcription of the lacZ gene driven by a cAMP-responsive element promoter. These data indicate that the composition of PKA in cortical and granule cells underlies the differential ability of these cells to transmit cAMP signals to the nucleus.  (+info)

Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450. (2/496)

A combination of protein kinase A type II (RII) overlay screening, database searches and PCR was used to identify a centrosomal A-kinase anchoring protein. A cDNA with an 11.7 kb open reading frame was characterized and found to correspond to 50 exons of genomic sequence on human chromosome 7q21-22. This cDNA clone encoded a 3908 amino acid protein of 453 kDa, that was designated AKAP450 (DDBJ/EMBL/GenBank accession No. AJ131693). Sequence comparison demonstrated that the open reading frame contained a previously characterized cDNA encoding Yotiao, as well as the human homologue of AKAP120. Numerous coiled-coil structures were predicted from AKAP450, and weak homology to pericentrin, giantin and other structural proteins was observed. A putative RII-binding site was identified involving amino acid 2556 of AKAP450 by mutation analysis combined with RII overlay and an amphipatic helix was predicted in this region. Immunoprecipitation of RII from RIPA-buffer extracts of HeLa cells demonstrated co-precipitation of AKAP450. By immunofluorecent labeling with specific antibodies it was demonstrated that AKAP450 localized to centrosomes. Furthermore, AKAP450 was shown to co-purify in centrosomal preparations. The observation of two mRNAs and several splice products suggests additional functions for the AKAP450 gene.  (+info)

Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220. (3/496)

The cyclic AMP (cAMP)-dependent protein kinase (PKA) and the type 1 protein phosphatase (PP1) are broad-specificity signaling enzymes with opposing actions that catalyze changes in the phosphorylation state of cellular proteins. Subcellular targeting to the vicinity of preferred substrates is a means of restricting the specificity of each enzyme [1] [2]. Compartmentalization of the PKA holoenzyme is mediated through association of the regulatory subunits with A-kinase anchoring proteins (AKAPs), whereas a diverse family of phosphatase-targeting subunits directs the location of the PP1 catalytic subunit (PP1c) [3] [4]. Here, we demonstrate that the PKA-anchoring protein, AKAP220, binds PP1c with a dissociation constant (KD) of 12.1 +/- 4 nM in vitro. Immunoprecipitation of PP1 from cell extracts resulted in a 10.4 +/- 3.8-fold enrichment of PKA activity. AKAP220 co-purified with PP1c by affinity chromatography on microcystin sepharos Immunocytochemical analysis demonstrated that the kinase, the phosphatase and the anchoring protein had distinct but overlapping staining patterns in rat hippocampal neurons. Collectively, these results provide the first evidence that AKAP220 is a multivalent anchoring protein that maintains a signaling scaffold of PP1 and the PKA holoenzyme.  (+info)

NH2-Terminal targeting motifs direct dual specificity A-kinase-anchoring protein 1 (D-AKAP1) to either mitochondria or endoplasmic reticulum. (4/496)

Subcellular localization directed by specific targeting motifs is an emerging theme for regulating signal transduction pathways. For cAMP-dependent protein kinase (PKA), this is achieved primarily by its association with A-kinase-anchoring proteins (AKAPs). Dual specificity AKAP1, (D-AKAP1) binds to both type I and type II regulatory subunits and has two NH2-terminal (N0 and N1) and two COOH-terminal (C1 and C2) splice variants (. J. Biol. Chem. 272:8057). Here we report that the splice variants of D-AKAP1 are expressed in a tissue-specific manner with the NH2-terminal motifs serving as switches to localize D-AKAP1 at different sites. Northern blots showed that the N1 splice is expressed primarily in liver, while the C1 splice is predominant in testis. The C2 splice shows a general expression pattern. Microinjecting expression constructs of D-AKAP1(N0) epitope-tagged at either the NH2 or the COOH terminus showed their localization to the mitochondria based on immunocytochemistry. Deletion of N0(1-30) abolished mitochondrial targeting while N0(1-30)-GFP localized to mitochondria. Residues 1-30 of N0 are therefore necessary and sufficient for mitochondria targeting. Addition of the 33 residues of N1 targets D-AKAP1 to the ER and residues 1-63 fused to GFP are necessary and sufficient for ER targeting. Residues 14-33 of N1 are especially important for targeting to ER; however, residues 1-33 alone fused to GFP gave a diffuse distribution. N1(14-33) thus serves two functions: (a) it suppresses the mitochondrial-targeting motif located within residues 1-30 of N0 and (b) it exposes an ER-targeting motif that is at least partially contained within the N0(1-30) motif. This represents the first example of a differentially targeted AKAP and adds an additional level of complexity to the PKA signaling network.  (+info)

Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus. (5/496)

A novel 450-kDa coiled-coil protein, CG-NAP (centrosome and Golgi localized PKN-associated protein), was identified as a protein that interacted with the regulatory region of the protein kinase PKN, having a catalytic domain homologous to that of protein kinase C. CG-NAP contains two sets of putative RII (regulatory subunit of protein kinase A)-binding motif. Indeed, CG-NAP tightly bound to RIIalpha in HeLa cells. Furthermore, CG-NAP was coimmunoprecipitated with the catalytic subunit of protein phosphatase 2A (PP2A), when one of the B subunit of PP2A (PR130) was exogenously expressed in COS7 cells. CG-NAP also interacted with the catalytic subunit of protein phosphatase 1 in HeLa cells. Immunofluorescence analysis of HeLa cells revealed that CG-NAP was localized to centrosome throughout the cell cycle, the midbody at telophase, and the Golgi apparatus at interphase, where a certain population of PKN and RIIalpha were found to be accumulated. These data indicate that CG-NAP serves as a novel scaffolding protein that assembles several protein kinases and phosphatases on centrosome and the Golgi apparatus, where physiological events, such as cell cycle progression and intracellular membrane traffic, may be regulated by phosphorylation state of specific protein substrates.  (+info)

Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex. (6/496)

Regulation of N-methyl-D-aspartate (NMDA) receptor activity by kinases and phosphatases contributes to the modulation of synaptic transmission. Targeting of these enzymes near the substrate is proposed to enhance phosphorylation-dependent modulation. Yotiao, an NMDA receptor-associated protein, bound the type I protein phosphatase (PP1) and the adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA) holoenzyme. Anchored PP1 was active, limiting channel activity, whereas PKA activation overcame constitutive PP1 activity and conferred rapid enhancement of NMDA receptor currents. Hence, yotiao is a scaffold protein that physically attaches PP1 and PKA to NMDA receptors to regulate channel activity.  (+info)

Conservation and function of a bovine sperm A-kinase anchor protein homologous to mouse AKAP82. (7/496)

Protein kinase A regulates sperm motility through the cAMP-dependent phosphorylation of proteins. One mechanism to direct the activity of the kinase is to localize it near its protein substrates through the use of anchoring proteins. A-Kinase anchoring proteins (AKAPs) act by binding the type II regulatory subunit of protein kinase A and tethering it to a cellular organelle or cytoskeletal element. We showed previously that mAKAP82, the major protein of the fibrous sheath of the mouse sperm flagellum, is an AKAP. The available evidence indicates that protein kinase A is compartmentalized to the fibrous sheath by binding mAKAP82. To characterize AKAP82 in bovine sperm, a testicular cDNA library was constructed and used to isolate a clone encoding bAKAP82, the bovine homologue. Sequence analysis showed that the primary structure of bAKAP82 was highly conserved. In particular, the amino acid sequence corresponding to the region of mAKAP82 responsible for binding the regulatory subunit of protein kinase A was identical in the bull. Bovine AKAP82 was present in both epididymal and ejaculated sperm and was localized to the entire principal piece of the flagellum, the region in which the fibrous sheath is located. Finally, bAKAP82 bound the regulatory subunit of protein kinase A. These data support the idea that bAKAP82 functions as an anchoring protein for the subcellular localization of protein kinase A in the flagellum.  (+info)

mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes. (8/496)

The compartmentalization of second messenger-activated protein kinases contributes to the fidelity of hormone-mediated signal transduction events. For example, the cAMP-dependent protein kinase is tethered at specific intracellular locations through association with A-kinase anchoring proteins (AKAPs). We now report the cloning of mAKAP, an anchoring protein found predominantly in heart, skeletal muscle and brain, and whose expression is induced in neonatal ventriculocytes by treatment with hypertrophic stimuli. mAKAP is targeted to the nuclear membrane of differentiated myocytes. Analysis of mAKAP-green fluorescent protein (GFP) fusion constructs revealed that nuclear membrane targeting is conferred by two regions of the protein, between residues 772-915 and 915-1065, which contain spectrin-like repeat sequences. Heterologous expression of the mAKAP targeting sequences displaced the endogenous anchoring protein from the nuclear membrane, demonstrating that mAKAP targeting is saturable. Collectively, these data suggest that a domain containing spectrin-like repeats mediates targeting of the anchoring protein mAKAP and the cAMP-dependent protein kinase holoenzyme to the nuclear membrane in response to differentiation signals.  (+info)

A kinase anchor protein (AKAP) is a type of scaffolding protein that plays a role in organizing and targeting various signaling molecules within cells. AKAPs are so named because they can bind to and anchor protein kinases, enzymes that add phosphate groups to other proteins, thereby modulating their activity. This allows for the localized regulation of signaling pathways and helps ensure that specific cellular responses occur in the correct location and at the right time. AKAPs can also bind to other signaling molecules, such as phosphatases, ion channels, and second messenger systems, forming large complexes that facilitate efficient communication between different parts of the cell.

There are many different AKAPs identified in various organisms, and they play crucial roles in a wide range of cellular processes, including cell division, signal transduction, and gene expression. Mutations or dysregulation of AKAPs have been implicated in several diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, understanding the structure, function, and regulation of AKAPs is an important area of research with potential therapeutic implications.

Cyclic AMP-dependent protein kinase RIIβ subunit, also known as PKA RIIβ or PRKAR2B, is a type of regulatory subunit of cyclic AMP (cAMP)-dependent protein kinase (PKA), which is a crucial enzyme in intracellular signaling pathways. The RIIβ subunit regulates the activity of PKA by binding to and inhibiting the catalytic subunits of the enzyme. When cAMP binds to the RIIβ subunit, it causes a conformational change that releases the catalytic subunits and activates the kinase. The RIIβ subunit is widely expressed in various tissues and plays a role in regulating diverse cellular processes, including metabolism, gene expression, and cell growth and differentiation.

Cyclic AMP-dependent protein kinase RIIα subunit, also known as PKA RIIα, is a regulatory subunit of the cyclic AMP (cAMP)-dependent protein kinase (PKA) enzyme complex. The cAMP-dependent protein kinase is a key enzyme in many signal transduction pathways and plays a crucial role in regulating various cellular processes, including metabolism, gene expression, and cell division.

The PKA enzyme complex consists of two regulatory subunits and two catalytic subunits. The RIIα subunit is one of the regulatory subunits that bind to cAMP, which leads to the release and activation of the catalytic subunits. Once activated, the catalytic subunits phosphorylate specific target proteins, thereby modulating their activity and function.

The RIIα subunit is expressed in many tissues and cell types, where it plays a role in regulating various physiological processes, such as cardiac contractility, neuronal excitability, and hormone secretion. Mutations in the gene encoding the RIIα subunit have been associated with several human diseases, including cancer, heart disease, and neurological disorders.

Cyclic AMP (cAMP)-dependent protein kinases, also known as protein kinase A (PKA), are a family of enzymes that play a crucial role in intracellular signaling pathways. These enzymes are responsible for the regulation of various cellular processes, including metabolism, gene expression, and cell growth and differentiation.

PKA is composed of two regulatory subunits and two catalytic subunits. When cAMP binds to the regulatory subunits, it causes a conformational change that leads to the dissociation of the catalytic subunits. The freed catalytic subunits then phosphorylate specific serine and threonine residues on target proteins, thereby modulating their activity.

The cAMP-dependent protein kinases are activated in response to a variety of extracellular signals, such as hormones and neurotransmitters, that bind to G protein-coupled receptors (GPCRs) or receptor tyrosine kinases (RTKs). These signals lead to the activation of adenylyl cyclase, which catalyzes the conversion of ATP to cAMP. The resulting increase in intracellular cAMP levels triggers the activation of PKA and the downstream phosphorylation of target proteins.

Overall, cAMP-dependent protein kinases are essential regulators of many fundamental cellular processes and play a critical role in maintaining normal physiology and homeostasis. Dysregulation of these enzymes has been implicated in various diseases, including cancer, diabetes, and neurological disorders.

Adaptor proteins are a type of protein that play a crucial role in intracellular signaling pathways by serving as a link between different components of the signaling complex. Specifically, "signal transducing adaptor proteins" refer to those adaptor proteins that are involved in signal transduction processes, where they help to transmit signals from the cell surface receptors to various intracellular effectors. These proteins typically contain modular domains that allow them to interact with multiple partners, thereby facilitating the formation of large signaling complexes and enabling the integration of signals from different pathways.

Signal transducing adaptor proteins can be classified into several families based on their structural features, including the Src homology 2 (SH2) domain, the Src homology 3 (SH3) domain, and the phosphotyrosine-binding (PTB) domain. These domains enable the adaptor proteins to recognize and bind to specific motifs on other signaling molecules, such as receptor tyrosine kinases, G protein-coupled receptors, and cytokine receptors.

One well-known example of a signal transducing adaptor protein is the growth factor receptor-bound protein 2 (Grb2), which contains an SH2 domain that binds to phosphotyrosine residues on activated receptor tyrosine kinases. Grb2 also contains an SH3 domain that interacts with proline-rich motifs on other signaling proteins, such as the guanine nucleotide exchange factor SOS. This interaction facilitates the activation of the Ras small GTPase and downstream signaling pathways involved in cell growth, differentiation, and survival.

Overall, signal transducing adaptor proteins play a critical role in regulating various cellular processes by modulating intracellular signaling pathways in response to extracellular stimuli. Dysregulation of these proteins has been implicated in various diseases, including cancer and inflammatory disorders.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Cyclic AMP-dependent protein kinase type II (PKA II) is a subtype of cyclic AMP (cAMP)-dependent protein kinase, which is a crucial enzyme in many cellular processes. PKA II is composed of two regulatory subunits and two catalytic subunits. When cAMP levels are low, the regulatory subunits bind to and inhibit the catalytic subunits. However, when cAMP levels rise, cAMP molecules bind to the regulatory subunits, causing a conformational change that releases and activates the catalytic subunits.

The activated catalytic subunits then phosphorylate specific serine and threonine residues on target proteins, thereby modulating their activity, localization, or stability. PKA II is widely expressed in various tissues and plays a role in regulating diverse cellular functions such as metabolism, gene expression, cell growth, differentiation, and apoptosis.

PKA II is distinct from the other subtype of cAMP-dependent protein kinase, PKA I, in its regulatory subunit composition and tissue distribution. While both PKA I and PKA II contain identical catalytic subunits, they differ in their regulatory subunits: PKA I contains the RIα, RIβ, or RIIβ regulatory subunits, while PKA II contains the RIIα regulatory subunit. Additionally, PKA II is predominantly expressed in tissues such as the brain, heart, and skeletal muscle, whereas PKA I is more widely distributed throughout the body.

Salivary alpha-amylases are a type of enzyme that are secreted by the salivary glands in humans and other mammals. These enzymes play a crucial role in the digestion of carbohydrates, specifically starches and glycogen, by breaking down these complex molecules into simpler sugars such as maltose, isomaltose, and maltotriose.

Salivary alpha-amylases are part of a larger family of enzymes known as alpha-amylases, which also include pancreatic alpha-amylases that are secreted by the pancreas and play a similar role in digestion. However, salivary alpha-amylases have some unique properties, such as being more resistant to denaturation by heat and acid than pancreatic alpha-amylases.

Salivary alpha-amylases are also used as a biomarker in forensic science for the identification of individuals, as they exhibit variations in their protein structure that can be used to distinguish between different people. Additionally, changes in salivary alpha-amylase levels have been associated with various physiological and psychological states, such as stress, anxiety, and arousal.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Seminal plasma proteins are a group of proteins that are present in the seminal fluid, which is the liquid component of semen. These proteins originate primarily from the accessory sex glands, including the prostate, seminal vesicles, and bulbourethral glands, and play various roles in the maintenance of sperm function and fertility.

Some of the key functions of seminal plasma proteins include:

1. Nutrition: Seminal plasma proteins provide energy sources and essential nutrients to support sperm survival and motility during their journey through the female reproductive tract.
2. Protection: These proteins help protect sperm from oxidative stress, immune attack, and other environmental factors that could negatively impact sperm function or viability.
3. Lubrication: Seminal plasma proteins contribute to the formation of a fluid medium that facilitates the ejaculation and transport of sperm through the female reproductive tract.
4. Coagulation and liquefaction: Some seminal plasma proteins are involved in the initial coagulation and subsequent liquefaction of semen, which helps ensure proper sperm release and distribution during ejaculation.
5. Interaction with female reproductive system: Seminal plasma proteins can interact with components of the female reproductive tract to modulate immune responses, promote implantation, and support early embryonic development.

Examples of seminal plasma proteins include prostate-specific antigen (PSA), prostate-specific acid phosphatase (PSAP), and semenogelins. Abnormal levels or dysfunctions in these proteins have been associated with various reproductive disorders, such as infertility, prostatitis, and prostate cancer.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Phosphatidylinositol 3-Kinases (PI3Ks) are a family of enzymes that play a crucial role in intracellular signal transduction. They phosphorylate the 3-hydroxyl group of the inositol ring in phosphatidylinositol and its derivatives, which results in the production of second messengers that regulate various cellular processes such as cell growth, proliferation, differentiation, motility, and survival.

PI3Ks are divided into three classes based on their structure and substrate specificity. Class I PI3Ks are further subdivided into two categories: class IA and class IB. Class IA PI3Ks are heterodimers consisting of a catalytic subunit (p110α, p110β, or p110δ) and a regulatory subunit (p85α, p85β, p55γ, or p50γ). They are primarily activated by receptor tyrosine kinases and G protein-coupled receptors. Class IB PI3Ks consist of a catalytic subunit (p110γ) and a regulatory subunit (p101 or p84/87). They are mainly activated by G protein-coupled receptors.

Dysregulation of PI3K signaling has been implicated in various human diseases, including cancer, diabetes, and autoimmune disorders. Therefore, PI3Ks have emerged as important targets for drug development in these areas.

Mitogen-activated protein kinase (MAPK) signaling system is a crucial pathway for the transmission and regulation of various cellular responses in eukaryotic cells. It plays a significant role in several biological processes, including proliferation, differentiation, apoptosis, inflammation, and stress response. The MAPK cascade consists of three main components: MAP kinase kinase kinase (MAP3K or MEKK), MAP kinase kinase (MAP2K or MEK), and MAP kinase (MAPK).

The signaling system is activated by various extracellular stimuli, such as growth factors, cytokines, hormones, and stress signals. These stimuli initiate a phosphorylation cascade that ultimately leads to the activation of MAPKs. The activated MAPKs then translocate into the nucleus and regulate gene expression by phosphorylating various transcription factors and other regulatory proteins.

There are four major MAPK families: extracellular signal-regulated kinases (ERK1/2), c-Jun N-terminal kinases (JNK1/2/3), p38 MAPKs (p38α/β/γ/δ), and ERK5. Each family has distinct functions, substrates, and upstream activators. Dysregulation of the MAPK signaling system can lead to various diseases, including cancer, diabetes, cardiovascular diseases, and neurological disorders. Therefore, understanding the molecular mechanisms underlying this pathway is crucial for developing novel therapeutic strategies.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Protein kinases are a group of enzymes that play a crucial role in many cellular processes by adding phosphate groups to other proteins, a process known as phosphorylation. This modification can activate or deactivate the target protein's function, thereby regulating various signaling pathways within the cell. Protein kinases are essential for numerous biological functions, including metabolism, signal transduction, cell cycle progression, and apoptosis (programmed cell death). Abnormal regulation of protein kinases has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.

Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.

A sarcomere is the basic contractile unit in a muscle fiber, and it's responsible for generating the force necessary for muscle contraction. It is composed of several proteins, including actin and myosin, which slide past each other to shorten the sarcomere during contraction. The sarcomere extends from one Z-line to the next in a muscle fiber, and it is delimited by the Z-discs where actin filaments are anchored. Sarcomeres play a crucial role in the functioning of skeletal, cardiac, and smooth muscles.

Hypertrophic cardiomyopathy (HCM) is a genetic disorder characterized by the thickening of the heart muscle, specifically the ventricles (the lower chambers of the heart that pump blood out to the body). This thickening can make it harder for the heart to pump blood effectively, which can lead to symptoms such as shortness of breath, chest pain, and fatigue. In some cases, HCM can also cause abnormal heart rhythms (arrhythmias) and may increase the risk of sudden cardiac death.

The thickening of the heart muscle in HCM is caused by an overgrowth of the cells that make up the heart muscle, known as cardiomyocytes. This overgrowth can be caused by mutations in any one of several genes that encode proteins involved in the structure and function of the heart muscle. These genetic mutations are usually inherited from a parent, but they can also occur spontaneously in an individual with no family history of the disorder.

HCM is typically diagnosed using echocardiography (a type of ultrasound that uses sound waves to create images of the heart) and other diagnostic tests such as electrocardiogram (ECG) and cardiac magnetic resonance imaging (MRI). Treatment for HCM may include medications to help manage symptoms, lifestyle modifications, and in some cases, surgical procedures or implantable devices to help prevent or treat arrhythmias.

Cardiac myosins are a type of myosin protein that are specifically expressed in the cardiac muscle cells (or cardiomyocytes) of the heart. These proteins play a crucial role in the contraction and relaxation of heart muscles, which is essential for proper heart function and blood circulation.

Myosins are molecular motors that use chemical energy from ATP to generate force and movement. In the context of cardiac muscle cells, cardiac myosins interact with another protein called actin to form sarcomeres, which are the basic contractile units of muscle fibers. During contraction, the heads of cardiac myosin molecules bind to actin filaments and pull them together, causing the muscle fiber to shorten and generate force.

There are different isoforms of cardiac myosins that can vary in their structure and function. Mutations in the genes encoding these proteins have been linked to various forms of cardiomyopathy, which are diseases of the heart muscle that can lead to heart failure and other complications. Therefore, understanding the structure and function of cardiac myosins is an important area of research for developing therapies and treatments for heart disease.

The myocardium is the middle layer of the heart wall, composed of specialized cardiac muscle cells that are responsible for pumping blood throughout the body. It forms the thickest part of the heart wall and is divided into two sections: the left ventricle, which pumps oxygenated blood to the rest of the body, and the right ventricle, which pumps deoxygenated blood to the lungs.

The myocardium contains several types of cells, including cardiac muscle fibers, connective tissue, nerves, and blood vessels. The muscle fibers are arranged in a highly organized pattern that allows them to contract in a coordinated manner, generating the force necessary to pump blood through the heart and circulatory system.

Damage to the myocardium can occur due to various factors such as ischemia (reduced blood flow), infection, inflammation, or genetic disorders. This damage can lead to several cardiac conditions, including heart failure, arrhythmias, and cardiomyopathy.

Myosins are a large family of motor proteins that play a crucial role in various cellular processes, including muscle contraction and intracellular transport. They consist of heavy chains, which contain the motor domain responsible for generating force and motion, and light chains, which regulate the activity of the myosin. Based on their structural and functional differences, myosins are classified into over 35 classes, with classes II, V, and VI being the most well-studied.

Class II myosins, also known as conventional myosins, are responsible for muscle contraction in skeletal, cardiac, and smooth muscles. They form filaments called thick filaments, which interact with actin filaments to generate force and movement during muscle contraction.

Class V myosins, also known as unconventional myosins, are involved in intracellular transport and organelle positioning. They have a long tail that can bind to various cargoes, such as vesicles, mitochondria, and nuclei, and a motor domain that moves along actin filaments to transport the cargoes to their destinations.

Class VI myosins are also unconventional myosins involved in intracellular transport and organelle positioning. They have two heads connected by a coiled-coil tail, which can bind to various cargoes. Class VI myosins move along actin filaments in a unique hand-over-hand motion, allowing them to transport their cargoes efficiently.

Overall, myosins are essential for many cellular functions and have been implicated in various diseases, including cardiovascular diseases, neurological disorders, and cancer.

Major Depressive Disorder (MDD), also simply referred to as depression, is a serious mental health condition characterized by the presence of one or more major depressive episodes. A major depressive episode is a period of at least two weeks during which an individual experiences a severely depressed mood and/or loss of interest or pleasure in nearly all activities, accompanied by at least four additional symptoms such as significant changes in appetite or weight, sleep disturbances, psychomotor agitation or retardation, fatigue or loss of energy, feelings of worthlessness or excessive guilt, difficulty thinking, concentrating, or making decisions, and recurrent thoughts of death or suicide.

MDD can significantly impair an individual's ability to function in daily life, and it is associated with increased risks of suicide, substance abuse, and other mental health disorders. The exact cause of MDD is not fully understood, but it is believed to result from a complex interplay of genetic, biological, environmental, and psychological factors. Treatment typically involves a combination of psychotherapy (such as cognitive-behavioral therapy) and medication (such as selective serotonin reuptake inhibitors or tricyclic antidepressants).

Mastodynia is a medical term that refers to breast pain or discomfort. This condition is often described as a dull, heavy, or burning sensation in the breast tissue. It can affect women of any age but is more common in those who are premenopausal, perimenopausal, or postmenopausal.

Mastodynia can be cyclical, meaning that it occurs at regular intervals and is often related to the menstrual cycle. Hormonal fluctuations during the cycle can cause breast tissue to become swollen and tender. Non-cyclical mastodynia, on the other hand, is not related to the menstrual cycle and may be caused by a variety of factors, such as breast cysts, trauma, or certain medications.

While mastodynia can be uncomfortable, it is usually not a sign of a serious medical condition. However, if you experience persistent or severe breast pain, it is important to speak with your healthcare provider to rule out any underlying causes and determine an appropriate course of treatment.

Sesquiterpenes are a class of terpenes that consist of three isoprene units and have the molecular formula C15H24. They are naturally occurring organic compounds that are synthesized by a variety of plants, insects, and other organisms. Sesquiterpenes play important roles in plant defense and communication, and some have been found to have medicinal properties.

Germacrane is a particular type of sesquiterpene that contains a specific carbon skeleton. It is a bicyclic compound with a five-membered ring fused to a seven-membered ring. Germacrane and its derivatives are found in various essential oils and have been studied for their potential therapeutic applications, including anti-inflammatory, antimicrobial, and anticancer activities.

Anisotropy is a medical term that refers to the property of being directionally dependent, meaning that its properties or characteristics vary depending on the direction in which they are measured. In the context of medicine and biology, anisotropy can refer to various biological structures, tissues, or materials that exhibit different physical or chemical properties along different axes.

For example, certain types of collagen fibers in tendons and ligaments exhibit anisotropic behavior because they are stronger and stiffer when loaded along their long axis compared to being loaded perpendicular to it. Similarly, some brain tissues may show anisotropy due to the presence of nerve fibers that are organized in specific directions, leading to differences in electrical conductivity or diffusion properties depending on the orientation of the measurement.

Anisotropy is an important concept in various medical fields, including radiology, neurology, and materials science, as it can provide valuable information about the structure and function of biological tissues and help guide diagnostic and therapeutic interventions.

Myelinated nerve fibers are neuronal processes that are surrounded by a myelin sheath, a fatty insulating substance that is produced by Schwann cells in the peripheral nervous system and oligodendrocytes in the central nervous system. This myelin sheath helps to increase the speed of electrical impulse transmission, also known as action potentials, along the nerve fiber. The myelin sheath has gaps called nodes of Ranvier where the electrical impulses can jump from one node to the next, which also contributes to the rapid conduction of signals. Myelinated nerve fibers are typically found in the peripheral nerves and the optic nerve, but not in the central nervous system (CNS) tracts that are located within the brain and spinal cord.

Diffusion Tensor Imaging (DTI) is a type of magnetic resonance imaging (MRI) technique that allows for the measurement and visualization of water diffusion in biological tissues, particularly in the brain. DTI provides information about the microstructural organization and integrity of nerve fibers within the brain by measuring the directionality of water diffusion in the brain's white matter tracts.

In DTI, a tensor is used to describe the three-dimensional diffusion properties of water molecules in each voxel (three-dimensional pixel) of an MRI image. The tensor provides information about the magnitude and direction of water diffusion, which can be used to calculate various diffusion metrics such as fractional anisotropy (FA), mean diffusivity (MD), axial diffusivity (AD), and radial diffusivity (RD). These metrics provide insights into the structural properties of nerve fibers, including their orientation, density, and integrity.

DTI has numerous clinical applications, such as in the diagnosis and monitoring of neurological disorders like multiple sclerosis, traumatic brain injury, and neurodegenerative diseases. It can also be used for presurgical planning to identify critical white matter tracts that need to be preserved during surgery.

Leukoencephalopathies are a group of medical conditions that primarily affect the white matter of the brain, which consists mainly of nerve fibers covered by myelin sheaths. These conditions are characterized by abnormalities in the structure and function of the white matter, leading to various neurological symptoms such as cognitive decline, motor impairment, seizures, and behavioral changes.

The term "leukoencephalopathy" is derived from two Greek words: "leukos," meaning white, and "enkephalos," meaning brain. The suffix "-pathy" refers to a disease or suffering. Therefore, leukoencephalopathies refer specifically to diseases that affect the white matter of the brain.

There are various types of leukoencephalopathies, including genetic, metabolic, infectious, toxic, and immune-mediated forms. Some examples include multiple sclerosis, adrenoleukodystrophy, Alexander disease, Canavan disease, and Marchiafava-Bignami disease. The diagnosis of leukoencephalopathies typically involves a combination of clinical evaluation, imaging studies such as MRI, and sometimes genetic or laboratory testing to identify the underlying cause. Treatment depends on the specific type and severity of the condition and may include medications, dietary modifications, physical therapy, or supportive care.

The A-kinase anchoring proteins or A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have ... Marin, Wenwen (January 2020). "A-kinase anchoring protein 1 (AKAP1) and its role in some cardiovascular diseases". Journal of ... Articles with short description, Short description matches Wikidata, A-kinase-anchoring proteins). ... AKAPs act as scaffold proteins wherein they bind PKA and other signaling proteins and physically tether these multi-protein ...
"Targeting of Protein Kinase A by Muscle A Kinase-anchoring Protein (mAKAP) Regulates Phosphorylation and Function of the ... It should not be confused with 5'-AMP-activated protein kinase (AMP-activated protein kinase). Protein kinase A, more precisely ... Protein kinase Signal transduction G protein-coupled receptor Serine/threonine-specific protein kinase Myosin light-chain ... out of 540 different protein kinase genes that make up the human kinome, only one other protein kinase, casein kinase 2, is ...
This gene encodes a member of the A-kinase anchoring protein (AKAP) family, a group of functionally related proteins that bind ... "A novel lipid-anchored A-kinase Anchoring Protein facilitates cAMP-responsive membrane events". The EMBO Journal. 17 (8): 2261- ... "Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein ... A-kinase anchor protein 7 isoform gamma is an enzyme that in humans is encoded by the AKAP7 gene. ...
2003). "Amino acid variant in the kinase binding domain of dual-specific A kinase-anchoring protein 2: a disease susceptibility ... "Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein ... "Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein ... A-kinase anchor protein 2 is an enzyme that in humans is encoded by the AKAP2 gene. AKAP2 has been shown to interact with ...
A-kinase anchor protein 8-like is a protein that in humans is encoded by the AKAP8L gene. AKAP8L has been shown to interact ... cloning and characterization of a novel nuclear protein, HA95, homologous to A-kinase anchoring protein 95". Biology of the ... "Entrez Gene: AKAP8L A kinase (PRKA) anchor protein 8-like". Yang JP, Tang H, Reddy TR, Wong-Staal F (Aug 2001). "Mapping the ... neighbor of A-kinase anchoring protein 95 (AKAP95) on chromosome 19p13.11-p13.12 region". Journal of Human Genetics. 45 (1): ...
A-kinase anchor protein 6 is an enzyme that in humans is encoded by the AKAP6 gene. The A-kinase anchor proteins (AKAPs) are a ... "Cloning and characterization of A-kinase anchor protein 100 (AKAP100). A protein that targets A-kinase to the sarcoplasmic ... "Entrez Gene: AKAP6 A kinase (PRKA) anchor protein 6". Marx, S O; Reiken S; Hisamatsu Y; Jayaraman T; Burkhoff D; Rosemblit N; ... Kapiloff MS, Schillace RV, Westphal AM, Scott JD (1999). "mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane ...
Howlett CJ, Robbins SM (March 2002). "Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular ... "The Cbl proteins are binding partners for the Cool/Pix family of p21-activated kinase-binding proteins". FEBS Lett. 550 (1-3): ... is a mammalian gene encoding the protein CBL which is an E3 ubiquitin-protein ligase involved in cell signalling and protein ... N-terminal tyrosine kinase binding domain (TKB domain): determines the protein which it can bind to RING finger domain motif: ...
Another protein essential for the SI response is MLPK, a serine-threonine kinase, which is anchored to the plasma membrane from ... Murase K, Shiba H, Iwano M, Che FS, Watanabe M, Isogai A, Takayama S (March 2004). "A membrane-anchored protein kinase involved ... The female determinant of the SI response in Brassica, is a transmembrane protein termed SRK, which has an intracellular kinase ... The interaction between the SRK and SCR/SP11 proteins results in autophosphorylation of the intracellular kinase domain of SRK ...
Chen L, Marquardt ML, Tester DJ, Sampson KJ, Ackerman MJ, Kass RS (2007). "Mutation of an A-kinase-anchoring protein causes ... Golgi reassembly-stacking proteins are an evolutionarily conserved family of proteins in the Golgi matrix. GRASP65 and GRASP55 ... encoding a transmembrane protein with a presumed role in vesicle-mediated sorting and intracellular protein transport". Am. J. ... The first individual protein component of the matrix was identified in 1995 as Golgin A2 (then called GM130). Since then, many ...
A-kinase anchor protein 5 is a protein that in humans is encoded by the AKAP5 gene. The A-kinase anchor proteins (AKAPs) are a ... 1995). "Association of protein kinase A and protein phosphatase 2B with a common anchoring protein". Science. 267 (5194): 108- ... "A-kinase anchoring protein 79/150 facilitates the phosphorylation of GABA(A) receptors by cAMP-dependent protein kinase via ... "Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins. ...
A-kinase anchor protein 8 is an enzyme that, in humans, is encoded by the AKAP8 gene. The A-kinase anchor proteins (AKAPs) are ... Collas P, Le Guellec K, Taskén K (Dec 1999). "The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in ... 2003). "Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication". J. Biol. Chem. 278 (29 ... Collas P, Le Guellec K, Taskén K (2000). "The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in ...
A-kinase anchor protein 12, aka AKAP250, is an enzyme that in humans is encoded by the AKAP12 gene. The A-kinase anchor ... Fan G, Shumay E, Wang H, Malbon CC (2001). "The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) ... "The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the beta 2-adrenergic receptor via the ... Piontek J, Brandt R (2003). "Differential and regulated binding of cAMP-dependent protein kinase and protein kinase C ...
A kinase anchor protein 10, mitochondrial is an enzyme that in humans is encoded by the AKAP10 gene. The A-kinase anchor ... Huang LJ, Durick K, Weiner JA, Chun J, Taylor SS (November 1997). "D-AKAP2, a novel protein kinase A anchoring protein with a ... a protein kinase A anchoring protein". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3220-5. Bibcode:2001PNAS...98.3220W. doi:10.1073/ ... "Amino acid variant in the kinase binding domain of dual-specific A kinase-anchoring protein 2: a disease susceptibility ...
A-kinase anchor protein 11 is an enzyme that in humans is encoded by the AKAP11 gene. The A-kinase anchor proteins (AKAPs) are ... "A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3beta (GSK-3beta ) and mediates protein kinase A-dependent ... "A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3beta (GSK-3beta ) and mediates protein kinase A-dependent ... Schillace RV, Scott JD (March 1999). "Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein ...
A-kinase anchor protein 4 is a scaffold protein that in humans is encoded by the AKAP4 gene. It involves in the intracellular ... The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to ... Brown PR, Miki K, Harper DB, Eddy EM (June 2003). "A-kinase anchoring protein 4 binding proteins in the fibrous sheath of the ... Brown PR, Miki K, Harper DB, Eddy EM (June 2003). "A-kinase anchoring protein 4 binding proteins in the fibrous sheath of the ...
Mochly-Rosen D (Apr 1995). "Localization of protein kinases by anchoring proteins: a theme in signal transduction". Science. ... Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the ... "Characterization of protein kinase C isotype expression in adult rat heart. Protein kinase C-epsilon is a major isotype present ... PRKCE protein kinase C, epsilon". Newton PM, Messing RO (Apr 2010). "The substrates and binding partners of protein kinase ...
Lea IA, Widgren EE, O'Rand MG (2004). "Association of sperm protein 17 with A-kinase anchoring protein 3 in flagella". Reprod. ... Frayne J, Hall L (2003). "A re-evaluation of sperm protein 17 (Sp17) indicates a regulatory role in an A-kinase anchoring ... Sperm surface protein Sp17 is a protein that in humans is encoded by the SPA17 gene. This gene encodes a protein present at the ... Studies in rabbits suggest that in sperm the protein is involved in fertilization by binding to the zona pellucida of the ...
"The A-kinase anchor protein AKAP121 is a negative regulator of cardiomyocyte hypertrophy". Journal of Molecular and Cellular ... "Induction of cardiomyocyte hypertrophy by specific knockdown of an a-kinase anchor protein". Journal of Molecular and Cellular ...
"Association of protein kinase A and protein phosphatase 2B with a common anchoring protein". Science. 267 (5194): 108-11. ... Calcineurin (CaN) is a calcium and calmodulin dependent serine/threonine protein phosphatase (also known as protein phosphatase ... Giri PR, Higuchi S, Kincaid RL (1991). "Chromosomal mapping of the human genes for the calmodulin-dependent protein phosphatase ... Frey N, Richardson JA, Olson EN (2000). "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins". Proc. Natl. ...
... evolutionarily conserved human gene family encoding proteins with presumptive protein kinase A anchoring function". Genomics. ... LRBA contains key features of both beige/CHS1 and A kinase anchor proteins (AKAPs; see MIM 602449).[supplied by OMIM] ... of a novel lipopolysaccharide-inducible gene with key features of both A kinase anchor proteins and chs1/beige proteins". J ... Lipopolysaccharide-responsive and beige-like anchor protein is a protein that in humans is encoded by the LRBA gene. Patients ...
The protein becomes activated when binding to receptors capable of protein kinase activity for cellular signaling. TGF-α is a ... As a membrane anchored-growth factor, TGF-α can be cleaved from an integral membrane glycoprotein via a protease. Soluble forms ... When TGF-α binds to EGFR it dimerizes triggering phosphorylation of a protein-tyrosine kinase. The activity of protein-tyrosine ... This protein may act as either a transmembrane-bound ligand or a soluble ligand. This gene has been associated with many types ...
Dart C, Leyland ML (2001). "Targeting of an A kinase-anchoring protein, AKAP79, to an inwardly rectifying potassium channel, ... The resulting protein eNpHR3.0 is used in optogenetic research to inhibit neurons with light. Expression of Kir2.1 gene in ... GeneReviews/NCBI/NIH/UW entry on Andersen-Tawil syndrome OMIM entries on Anderson-Tawil syndrome KCNJ2+protein,+human at the U. ... Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): ...
Ulfig N, Chan WY (2003). "Expression of a kinase anchoring protein 79 and synaptophysin in the developing human red nucleus". ... The encoded protein has 313 amino acids with a predicted molecular weight of 33.845 kDa. The protein is a synaptic vesicle ... Synaptophysin, also known as the major synaptic vesicle protein p38, is a protein that in humans is encoded by the SYP gene. ... The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when ...
Diviani D, Langeberg LK, Doxsey SJ, Scott JD (Apr 2000). "Pericentrin anchors protein kinase A at the centrosome through a ... protein kinase A, protein kinase C, DISC1, γ-tubulin complex proteins, and PCM1. GRCh38: Ensembl release 89: ENSG00000160299 - ... This protein localizes to the centrosome and recruits proteins to the pericentriolar matrix (PCM) to ensure proper centrosome ... which is a centrosome scaffold that anchors microtubule nucleating complexes and other centrosomal proteins. In one model, PCNT ...
"Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in ... "FER - Receptor-like protein kinase FERONIA precursor - Arabidopsis thaliana (Mouse-ear cress) - FER gene & protein". www. ... Feronia, also known as FER or protein Sirene, is a recognition receptor kinase found in plants. FER plays a significant part in ... FER is one of the known 17 proteins which play a part in Arabidopsis Catharanthus roseus RLK1-like kinases (CrRLK1Ls). ...
A-kinase-anchoring proteins (AKAPs) bind a surface formed between both R subunits and target the kinase to different locations ... Protein kinase A catalytic subunit (PKA Cα) is a member of the AGC kinase family (protein kinases A, G, and C), and contributes ... Snyder EM, Colledge M, Crozier RA, Chen WS, Scott JD, Bear MF (Apr 2005). "Role for A kinase-anchoring proteins (AKAPS) in ... This led to the hypothesis that the subcellular localization of anchored PKA controls what proteins are regulated by the kinase ...
Mochly-Rosen D (April 1995). "Localization of protein kinases by anchoring proteins: a theme in signal transduction". Science. ... "Protein kinase C-associated kinase (PKK), a novel membrane-associated, ankyrin repeat-containing protein kinase". The Journal ... Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene. Protein kinase C (PKC) is a family of ... December 1996). "Protein-protein interaction of zinc finger LIM domains with protein kinase C". The Journal of Biological ...
The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway ... Li S, Couet J, Lisanti MP (November 1996). "Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored ... Caveolin 1 has been shown to interact with heterotrimeric G proteins, Src tyrosine kinases (Src, Lyn) and H-Ras,cholesterol,TGF ... Caveolin-1 is a protein that in humans is encoded by the CAV1 gene. The scaffolding protein encoded by this gene is the main ...
"Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex". Mol. ... "Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)". Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y (Sep 2002 ... Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene. Calmodulin 1 is the archetype of the family of calcium- ... Gusev NB (2002). "Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth ...
Diviani D, Soderling J, Scott JD (November 2001). "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho- ... Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". The Journal of ... Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". The Journal of ... Ras homolog gene family, member B, also known as RHOB, is a protein which in humans is encoded by the RHOB gene. RHOB is a ...
Interaction of glycosyl-phosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn 1". Journal of Immunology. ... 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: the p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase". ... Lck (or lymphocyte-specific protein tyrosine kinase) is a 56 kDa protein that is found inside specialized cells of the immune ... "The glycophosphatidylinositol-anchored Thy-1 molecule interacts with the p60fyn protein tyrosine kinase in T cells". The ...
PMID 27057472 A-kinase anchor protein 4 (AKAP4) a promising therapeutic target of colorectal cancer. Jagadish N, Parashar D, ... PMID 20564126 Gene silencing of A-kinase anchor protein 4 inhibits cervical cancer growth in vitro and in vivo. Saini S, ... PMID 19190149 A novel cancer testis antigen, A-kinase anchor protein 4 (AKAP4) is a potential biomarker for breast cancer. ... PMID 17332284 A novel cancer testis antigen, A-kinase anchor protein 4 (AKAP4) is a putative target for immunotherapy of ...
"Down-regulation of tumor suppressor A kinase anchor protein 12 in human hepatocarcinogenesis by epigenetic mechanisms". ...
The A-kinase anchoring proteins or A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have ... Marin, Wenwen (January 2020). "A-kinase anchoring protein 1 (AKAP1) and its role in some cardiovascular diseases". Journal of ... Articles with short description, Short description matches Wikidata, A-kinase-anchoring proteins). ... AKAPs act as scaffold proteins wherein they bind PKA and other signaling proteins and physically tether these multi-protein ...
... a member of the A Kinase Anchor Protein (AKAP) family of polypeptides that bind the regulatory (RII) subunit of protein kinase ... a member of the A Kinase Anchor Protein (AKAP) family of polypeptides that bind the regulatory (RII) subunit of protein kinase ... a member of the A Kinase Anchor Protein (AKAP) family of polypeptides that bind the regulatory (RII) subunit of protein kinase ... a member of the A Kinase Anchor Protein (AKAP) family of polypeptides that bind the regulatory (RII) subunit of protein kinase ...
Knockout of A-kinase anchoring protein GSKIP in mice causes perinatal lethality. Title: Knockout of A-kinase anchoring protein ... A-kinase anchoring proteins (AKAPs) control the localization of cAMP-dependent protein kinase A (PKA) and tether PKA to ... Knockout of A-kinase anchoring protein GSKIP in mice causes perinatal lethality. *Login ... AKAPs engage in protein-protein interactions with PKA substrates and other signalling proteins and form multi-protein complexes ...
located_in anchoring junction IEA Inferred from Electronic Annotation. more info. located_in axon ISO Inferred from Sequence ... MAP kinase 1. MAP kinase 2. MAPK 1. MAPK 2. extracellular signal-regulated kinase 2. mitogen-activated protein kinase 2. p42- ... enables mitogen-activated protein kinase kinase kinase binding ISO Inferred from Sequence Orthology. more info ... Mapk1 mitogen-activated protein kinase 1 [Mus musculus] Mapk1 mitogen-activated protein kinase 1 [Mus musculus]. Gene ID:26413 ...
Efficient phosphorylation requires that PKA be anchored close to its targets by A-kinase anchoring proteins (AKAPs). Cardiac ... As MMGL has previously been shown to interact with phosphodiesterase 4D, we speculated that it may be a PKA-anchoring protein ( ... the ability of MMGL isoform 4 to interact with PKA regulatory subunits R1A and R2A using Y2H-based direct protein-protein ... causing sarcomeric proteins which regulate contractility in response to PKA phosphorylation. During a yeast 2-hybrid (Y2H) ...
1998) The A kinase anchoring protein is required for mediating the effect of protein kinase A on ROMK1 channels. Proc Natl Acad ... 1999) The A-kinase anchor protein MAP2B and cAMP-dependent protein kinase are associated with class C L-type calcium channels ... 1997a) D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain. Proc Natl Acad Sci USA 94:11184-11189. ... 1997b) Identification of a novel protein kinase A anchoring protein that binds both type I, type II regulatory subunits. J Biol ...
... protein kinase C epsilon phosphorylation sites in P; CK II, casein kinase phosphorylation sites in P; SIG, signal peptide; ... Furin, furin cleavage site; TM, transmembrane anchor of G; A - D, conserved RNA-dependent RNA polymerase motifs. Conserved ... N, nucleoprotein; P, phosphoprotein; X, X protein; M, matrix protein; G, glycoprotein; L, L-polymerase protein. Genome regions ... Conservation of genome organization, regulatory sequences, and protein domains of Borna disease virus (BDV) in novel strains ...
The A-kinase anchoring protein 79/150 (AKAP79/150) signaling scaffold regulates AMPAR phosphorylation, channel activity, and ... Palmitoylation of A-kinase anchoring protein 79/150 regulates dendritic endosomal targeting and synaptic plasticity mechanisms. ...
A-kinase anchoring protein 95 (AKAP95). ENSAMEP00000000344. PF07535. 0.00033. zf-DBF. DBF zinc finger. ... Protein. Program. Term. IPRS. Start. End. Score. Description. ENSAMEP00000000344. ProSitePatterns. PS00028. IPR007087. 159. 181 ...
A-kinase anchor protein 12 (AKAP12; also known as Gravin) functions as a tumor suppressor in several human primary cancers. ... protein binding - protein deacetylase activity - protein deacetylation - regulation of mitotic cell cycle - regulation of ... Finally, a protein-protein interaction (PPI) network was constructed, as well as functional annotation and pathway enrichment ... C-terminal binding protein (CtBP) interacting protein (CtIP). These SFN analogs also altered HAT/HDAC activities and histone ...
A-kinase anchoring protein 9. ISO. RGD. PMID:18772391. RGD:2313147. NCBI chr 7:83,942,590...84,108,648 Ensembl chr 7:97,540,356 ... A-kinase anchoring protein 5. ISO. RGD. PMID:20410303. RGD:7242424. NCBI chr14:45,045,476...45,050,946 Ensembl chr14:63,302,200 ... A-kinase anchoring protein 6. ISO. RGD. PMID:19574217. RGD:6902943. NCBI chr14:12,978,221...13,602,732 Ensembl chr14:31,395,026 ... A-kinase anchoring protein 5. ISO. RGD. PMID:20410303. RGD:7242424. NCBI chr14:45,045,476...45,050,946 Ensembl chr14:63,302,200 ...
Name: A kinase anchor protein 13. Synonyms: AKAP-Lbc, PROTO-LBC, PROTO-LB, Ht31, 5730522G15Rik, 1700026G02Rik, 5830460E08Rik ...
... protein was found downregulated across the grades. AKAP12 knockdown in benign meningioma cells SF4433 increases proliferation, ... In the discovery set of fresh-frozen tissue specimens (14), the A-kinase anchor protein 12 (AKAP12) ... In the discovery set of fresh-frozen tissue specimens (14), the A-kinase anchor protein 12 (AKAP12) protein was found ... Down-Regulation of Tumor Suppressor A Kinase Anchor Protein 12 in Human Hepatocarcinogenesis by Epigenetic Mechanisms. ...
Isolation and molecular characterization of AKAP110, a novel, sperm-specific protein kinase A-anchoring protein. Mol Endocrinol ... Protein kinase A-anchoring inhibitor peptides arrest mammalian sperm motility. J Biol Chem. 1997 Feb 21;272(8):4747-52.[PubMed] ... protein 14-3-3 and a protein kinase, glycogen synthase kinase 3 (GSK-3). ... Subcellular localization of the regulatory subunits of cyclic adenosine 3,5-monophosphate-dependent protein kinase in bovine ...
Gpr161 is an A-kinase anchoring protein and the cAMP-sensing Gpr161:PKA complex acts as cilium-compartmentalized signalosome ... General protein information Go to the top of the page Help Preferred Names. G-protein coupled receptor 161. Names. G-protein ... The protein encoded by this gene is an orphan G protein-coupled receptor whose ligand is unknown. This gene is overexpressed in ... mRNA and Protein(s) * NM_001267609.1 → NP_001254538.1 G-protein coupled receptor 161 isoform 1 ...
... nuclear proteins, chaperones, Alzheimer disease-related proteins, oxidative stress proteins, kinases, and neuronal proteins. [ ... Myotilin protein binds to α-actinin, filamin C, and actin, and it is likely important in stabilizing and anchoring thin ... Telethonin protein (titin-cap protein) is a sarcomeric protein present in the Z disk that binds to titin and several other Z- ... Dysferlin protein is a large membrane protein with sequence analogy to the nematode protein fer-1, and is a member of the ...
A kinase (PRKA) anchor protein 7. ALDH8A1. 64577. 6q23.2. 135238528. 135271260. 32732. REVIEWED. aldehyde dehydrogenase 8 ... mitogen-activated protein kinase kinase kinase 5. MAP7. 9053. 6q23.3. 136663872. 136871792. 207920. REVIEWED. microtubule- ... ribosomal protein L15 pseudogene 9. RPL17P23. 100271152. 6q22.33. 127756759. 127757360. 601. INFERRED. ribosomal protein L17 ... ribosomal protein L21 pseudogene 64. RPL21P66. 100271179. 6q23. 132839950. 132840470. 520. INFERRED. ribosomal protein L21 ...
Jones, R.G.; Plas, D.R.; Kubek, S.; Buzzai, M.; Mu, J.; Xu, Y.; Birnbaum, M.J.; Thompson, C.B. AMP-activated protein kinase ... Li, S.; Couet, J.; Lisanti, M.P. Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding ... Such prenylation has important roles in the generation of lipidated protein domains that enable protein-protein interactions ... Hardie, D.G. The AMP-activated protein kinase pathway-New players upstream and downstream. J. Cell Sci. 2004, 117, 5479-5487. [ ...
... and discuss how this molecule infl uences the retention and clustering of diverse synaptic proteins to regulate synaptic ... and discuss how this molecule influences the retention and clustering of diverse synaptic proteins to regulate synaptic ... Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins: ... localization regulated by NMDA receptor activation through translocation of an A-kinase anchoring protein scaffold protein. J. ...
A Kinase Anchor Proteins:physiology, Animals, Humans, Signal Transduction:physiology,. Citation OBJECTIVE: Kinase Anchoring ... Proteins (AKAPs) have evolved to regulate the spatial and temporal organization of cellular signal transductio..... ...
A Kinase Anchor Proteins:physiology, Animals, Humans, Signal Transduction:physiology,. Citation OBJECTIVE: Kinase Anchoring ... Protein Processing, Post-Translational:physiology, RNA, Messenger:genetics, RNA, Small Interfering:genetics,. Citation ... Proteins (AKAPs) have evolved to regulate the spatial and temporal organization of cellular signal transductio..... ...
... binds the glycosylphosphatidylinositol-anchored protein GFRα3 and the receptor tyrosine kinase Ret. Expression of the GFRα3 ... Artemin activates src-family kinase-dependent cell-signaling pathways after binding to its GFRα3 and Ret kinase receptor ... activate the Ret receptor tyrosine kinase through binding of glycosylphosphatidylinositol-anchored GDNF family receptor α ... The TRPA1 channel protein is a marker for GFRα3 neurons and is modulated by artemin level. In addition to TRPV1, increased skin ...
... and regulation of ryanodine receptors and A-kinase anchoring proteins. We initially identified vertebrate Clic4 as a candidate ... CLIC proteins might have several biochemical functions including intracellular chloride channel activity, modulation of ...
Poppinga WJ, Munoz-Llancao P, Gonzalez-Billault C, Schmidt M: A-kinase anchoring proteins: cAMP compartmentalization in ... AKAP7 encodes protein family binding to a regulatory subunit (RII) of cAMP-dependent protein kinase A (PKA); sElevation of cAMP ... For instance, ATF7IP can form a protein-complex by binding to MBD1 (methyl CpG binding protein 1) and Aire (autoimmune ... ATF7IP can interact with methyl CpG binding protein 1 (MBD1) and the autoimmune regulator (Aire) protein to maintain immune ...
CoMSIA studies on substituted ureas as Raf-1 kinase inhibitors and its confirmation with structure-based studies. Download ... The 4-pyridyl group bearing amide substituent is located in the adenosine binding pocket, and anchored to the protein through a ... 3D-QSAR studies on c-Src kinase inhibitors and docking analyses of a potent dual kinase inhibitor of c-Src and c-Abl kinases. ... MolecularProtein BindingProto-Oncogene Proteins B-rafProto-Oncogene Proteins c-rafQuantitative Structure-Activity Relationship ...
... the serine-arginine protein kinase SRPK2 [126]; GPCR-associated sorting protein 2 (GPRASP2), implicated in ciliary ... a ALMS1 has been implicated in anchoring the centrosome cohesion protein C-Nap1/CEP250 to centriole proximal ends [21], akin to ... Protein-protein interactions and proximity interactions. Numerous candidate ALMS1-interacting proteins have been reported. ... a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2. J Cell Biol ...
... family of kinases may have assumed distinct responsibilities for the control of complex and diverse cellular f ... Individual isoforms of the protein kinase C (PKC) ... this protein-protein interaction securely anchored PKC epsilon ... Individual isoforms of the protein kinase C (PKC) family of kinases may have assumed distinct responsibilities for the control ... Thus, actin appears to be a bifunctional anchoring protein that is specific for the PKC epsilon isoform. The assembly of this ...
GTP-bound Ras activates Raf to trigger a phosphorylation cascade involving mitogen-activated protein kinases (MEKs). This ... Ras is a GTPase that is anchored to the intracellular side of the plasma membrane through its post-translational lipid ... and protein kinase C (PKC). Ras activated by this mechanism drives the PI3K pathway to initiate expression of cell growth genes ... This causes adaptor protein GRB2 to recruit SOS, a guanine nucleotide exchange factor, which then facilitates binding of GTP to ...
A-kinase anchoring protein 17A [Sou.... AKAP8. 10270. AKAP8. A-kinase anchoring protein 8 [Sourc.... ... We found that a number of Tfh cells downmodulated BCL6 protein after their development, and we sought to compare the gene ...
PKD1 has two C1 domains, which both bind to diacylglycerol, serving as membrane anchors. Binding of DAG is a required step in ... Rapid protein kinase D translocation in response to G protein-coupled receptor activation. Dependence on protein kinase C. J. ... Oxidative stress induces protein kinase D activation in intact cells. Involvement of Src and dependence on protein kinase C. J ... The serine/threonine kinase protein kinase D1 (PKD1) is a stress-responsive kinase and sensor for reactive oxygen species, ...
  • Cardiac contractility is regulated by dynamic phosphorylation of sarcomeric proteins by kinases such as cAMP-activated protein kinase A (PKA). (biomedcentral.com)
  • Efficient phosphorylation requires that PKA be anchored close to its targets by A-kinase anchoring proteins (AKAPs). (biomedcentral.com)
  • Cardiac Myosin Binding Protein-C (cMyBPC) and cardiac troponin I (cTNI) are hypertrophic cardiomyopathy (HCM)-causing sarcomeric proteins which regulate contractility in response to PKA phosphorylation. (biomedcentral.com)
  • The potentiation was prevented in the presence of the selective PKA inhibitor PKI 14-22 , suggesting PKA-mediated phosphorylation of the heat transducer protein. (jneurosci.org)
  • The A-kinase anchoring protein 79/150 (AKAP79/150) signaling scaffold regulates AMPAR phosphorylation , channel activity, and endosomal trafficking associated with LTP and LTD. AKAP79/150 is targeted to dendritic spine plasma membranes by an N-terminal polybasic domain that binds phosphoinositide lipids , F-actin , and cadherin cell adhesion molecules . (bvsalud.org)
  • To map the mechanisms of aggressiveness we aimed to investigate changes in protein phosphorylation across WHO grades of human meningiomas. (nature.com)
  • Using gene knockout, transgenic and molecular approaches we are investigating the signal mechanisms underlying regulation of protein phosphorylation and sperm function. (kent.edu)
  • Snow AJ, Puri P, Acker-Palmer A, Bouwmeester T, Vijayaraghavan S, Kline D. Phosphorylation-dependent interaction of tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein (YWHA) with PADI6 following oocyte maturation in mice.Biol Reprod. (kent.edu)
  • GTP-bound Ras activates Raf to trigger a phosphorylation cascade involving mitogen-activated protein kinases (MEKs). (biolegend.com)
  • Tau phosphorylation regulates both normal and pathological functions of this protein. (biovendor.com)
  • Gene therapy displacement of endogenous MCUb with a dominant-negative MCUb transgene (MCUb W246R/V251E ) in vivo rescued T2D cardiomyocytes from metabolic inflexibility and stimulated cardiac contractile function and adrenergic responsiveness by enhancing phospholamban phosphorylation via protein kinase A. We conclude that MCUb represents one newly discovered molecular effector at the interface of metabolism and cardiac function, and its repression improves the outcome of the chronically stressed diabetic heart. (diabetesjournals.org)
  • The compounds have been found to regulate phospholamban phosphorylation by interfering with the A-kinase anchor protein 18delta (AKAP185) binding to the PKA substrate phospholamban. (justia.com)
  • The dimerization and docking (D/D) domain of the regulatory subunit dimer of PKA binds with the A-kinase binding (AKB) domain (an amphipathic helix) of AKAP. (wikipedia.org)
  • The subject of the study was the major fibrous sheath protein of the mouse sperm flagellum, AKAP82, a member of the A Kinase Anchor Protein (AKAP) family of polypeptides that bind the regulatory (RII) subunit of protein kinase A (PK-A). Immunoelectron microscopy demonstrated that AKAP82 is present throughout the transverse ribs and longitudinal columns of the fibrous sheath. (elsevierpure.com)
  • Glycogen synthase 3β (GSK3β) interaction protein (GSKIP) was identified as an AKAP by our group. (fu-berlin.de)
  • A-Kinase-Ankerproteine (AKAP) bilden durch direkte Protein-Protein- Interaktionen mit der cAMP-abhängigen Proteinkinase A (PKA), PKA-Substraten sowie weiteren Signalproteinen Multiproteinkomplexe und verankern diese an spezifischen intrazellulären Kompartimenten. (fu-berlin.de)
  • Glycogen synthase 3β (GSK3β) interaction protein (GSKIP) wurde von unserer Arbeitsgruppe als neues AKAP identifiziert. (fu-berlin.de)
  • As MMGL has previously been shown to interact with phosphodiesterase 4D, we speculated that it may be a PKA-anchoring protein (AKAP). (biomedcentral.com)
  • The translocation and the current potentiation were abolished in the presence of an A-kinase anchoring protein (AKAP) inhibitor. (jneurosci.org)
  • The A-kinase anchoring proteins or A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. (wikipedia.org)
  • AKAPs act as scaffold proteins wherein they bind PKA and other signaling proteins and physically tether these multi-protein complexes to specific locations, such as the nucleus, in cells. (wikipedia.org)
  • A-kinase anchoring proteins (AKAPs) control the localization of cAMP-dependent protein kinase A (PKA) and tether PKA to distinct cellular compartments. (fu-berlin.de)
  • In addition, AKAPs engage in protein-protein interactions with PKA substrates and other signalling proteins and form multi-protein complexes. (fu-berlin.de)
  • Kinase Anchoring Proteins (AKAPs) have evolved to regulate the spatial and temporal organization of cellular signal transductio. (nel.edu)
  • The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. (thermofisher.com)
  • A-kinase anchoring proteins (AKAPs) 9 1.5.1. (fu-berlin.de)
  • A kinase anchoring proteins (AKAPs) anchor PKA to its substrates and contribute to the specificity of signaling by compartmentalizing PKA and other signaling molecules [Wong, Scott 04]. (fu-berlin.de)
  • Artemin, a neuronal survival factor in the glial cell line-derived neurotrophic factor family, binds the glycosylphosphatidylinositol-anchored protein GFRα3 and the receptor tyrosine kinase Ret. (jneurosci.org)
  • GDNF family ligands (GFLs) activate the Ret receptor tyrosine kinase through binding of glycosylphosphatidylinositol-anchored GDNF family receptor α coreceptors (GFRα1-4) ( Sariola and Saarma, 2003 ). (jneurosci.org)
  • The receptor tyrosine kinase RET is a member of the cadherin superfamily. (thermofisher.cn)
  • The serine/threonine kinase protein kinase D1 (PKD1) is a stress-responsive kinase and sensor for reactive oxygen species, which can initiate cell survival through NF-κB signaling. (biologists.com)
  • AKT serine/threonine kinase 3. (gsea-msigdb.org)
  • Angelisová P, Drbal K, Horejsí V, Cerný J: Association of CD10/neutral endopeptidase 24.11 with membrane microdomains rich in glycosylphosphatidylinositol-anchored proteins and Lyn kinase. (exbio.cz)
  • Expression of the GFRα3 receptor is primarily restricted to the peripheral nervous system and is found in a subpopulation of nociceptive sensory neurons of the dorsal root ganglia (DRGs) that coexpress the Ret and TrkA receptor tyrosine kinases and the thermosensitive channel TRPV1. (jneurosci.org)
  • Upon stimulation by growth factors, cytokines, neurotransmitters, or other signals, receptor tyrosine kinases on the cell surface will be autophosphorylated. (biolegend.com)
  • In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. (embl.de)
  • A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A subtypes to distinct subcellular sites. (bvsalud.org)
  • What pathways are this gene/protein implicaed in? (cancerindex.org)
  • Limb-girdle muscular dystrophy (LGMD) protein defects occur in several pathways involved in the biologic function of muscle and can be divided into groups based on cellular localization. (medscape.com)
  • Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function. (rupress.org)
  • Protein kinase A type II activation is sufficient to control the cellular localization of the water channel aquaporin-2 in the kidney 72 3.3.1. (fu-berlin.de)
  • Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins. (lu.se)
  • Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with a cytoplasmically oriented CTP-binding site. (medlineplus.gov)
  • The membrane protein muscle-specific tyrosine kinase (MuSK) has been identified as the target of antibody attack in approximately 40% of patients with seronegative myasthenia gravis. (medscape.com)
  • ß-Adrenergic stimulation regulates cardiac contractility through a cyclic adenosine monophosphate (cAMP)- and protein kinase A (PKA)- dependent signaling pathway. (fu-berlin.de)
  • It associates with protein kinases A and C and phosphatase, and serves as a scaffold protein in signal transduction. (thermofisher.com)
  • Canonical Notch signaling activates the transcription of BMI1 proto‑oncogene polycomb ring finger, cyclin D1, CD44, cyclin dependent kinase inhibitor 1A, hes family bHLH transcription factor 1, hes related family bHLH transcription factor with YRPW motif 1, MYC, NOTCH3, RE1 silencing transcription factor and transcription factor 7 in a cellular context‑dependent manner, while non‑canonical Notch signaling activates NF‑κB and Rac family small GTPase 1. (spandidos-publications.com)
  • Huang Z, Somanath PR, Chakrabarti R, Eddy EM, Vijayaraghavan S. Changes in intracellular distribution and activity of protein phosphatase PP1gamma2 and its regulating proteins in spermatozoa lacking AKAP4. (kent.edu)
  • CLIC proteins might have several biochemical functions including intracellular chloride channel activity, modulation of transforming growth factor (TGF)-β signaling, and regulation of ryanodine receptors and A-kinase anchoring proteins. (nih.gov)
  • Ras is a GTPase that is anchored to the intracellular side of the plasma membrane through its post-translational lipid modifications. (biolegend.com)
  • Tau interacts with actin in the cytoskeleton and neuronal outgrowth, anchors enzymes such as protein kinases and phosphatases, and regulates intracellular vesicle transport. (biovendor.com)
  • For example, prostaglandins activate G s -protein-coupled receptors and initiate cAMP- and protein kinase A (PKA)-mediated processes. (jneurosci.org)
  • In line with a more complex picture, multiple isoforms of the protein likely exist and non-centrosomal sites of localisation have been reported. (springer.com)
  • Individual isoforms of the protein kinase C (PKC) family of kinases may have assumed distinct responsibilities for the control of complex and diverse cellular functions. (rupress.org)
  • However, since these kinases regulate a broad range of cellular responses, their compartmentalization in close proximity to their sarcomeric targets is required to facilitate control over which proteins are phosphorylated in response to second messenger signalling [ 8 , 9 ]. (biomedcentral.com)
  • This protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. (cancerindex.org)
  • In this review we will highlight mechanisms that control targeting of PSD-95 at the synapse, and discuss how this molecule influences the retention and clustering of diverse synaptic proteins to regulate synaptic structure and strength. (frontiersin.org)
  • They play a role in focusing the PROTEIN KINASE A activity toward relevant substrates. (bvsalud.org)
  • One such protein is AKAP5 (previously AKAP79), which contains SLiMs that anchor PKA and Calcineurin, and recruit substrate (the TRPV1 receptor). (kcl.ac.uk)
  • Calcineurin is anchored to AKAP5 by a well-characterised PxIxIT SLiM. (kcl.ac.uk)
  • Palmitoylation of A-kinase anchoring protein 79/150 regulates dendritic endosomal targeting and synaptic plasticity mechanisms. (bvsalud.org)
  • New mutations have been found in the synaptic nuclear envelope protein 1 ( SYNE1 ) gene and in the synaptic nuclear envelope protein 2 ( SYNE2 ) gene in a few families, also termed Nesprin-1 and Nesprin-2, respectively. (medscape.com)
  • Protein regulators of this enzyme include inhibitors I2 (PPP1R2) and I3 (PPP1R11), sds22 (PPP1R7), protein 14-3-3 and a protein kinase, glycogen synthase kinase 3 (GSK-3). (kent.edu)
  • It is also compatible with the requirement for both stable anchoring of the enzyme and responsive downstream signalling. (kcl.ac.uk)
  • The DOLK gene provides instructions for making the dolichol kinase enzyme, which facilitates the final step of the production of a compound called dolichol phosphate. (medlineplus.gov)
  • DOLK gene mutations change single protein building blocks (amino acids) in the dolichol kinase enzyme, leading to an enzyme with reduced or absent activity. (medlineplus.gov)
  • To investigate this possibility, we assessed the ability of MMGL isoform 4 to interact with PKA regulatory subunits R1A and R2A using Y2H-based direct protein-protein interaction assays. (biomedcentral.com)
  • Conservation of genome organization, regulatory sequences, and protein domains of Borna disease virus (BDV) in novel strains from parrots 1034, 1322, and 1367. (cdc.gov)
  • The binding of PKC epsilon to actin required that the kinase be activated, presumably to expose a cryptic binding site that we have identified and shown to be located between the first and second cysteine-rich regions within the regulatory domain of only this individual isoform of PKC. (rupress.org)
  • Over fifty members of this family exist, most of which bind specifically to regulatory subunits of CYCLIC AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. (bvsalud.org)
  • Emerin is a ubiquitous inner nuclear membraneprotein, presentin nearly all cell types, although its highest expression is in skeletal and cardiacmuscle.Emerin binds to many nuclear proteins, including several gene-regulatory proteins (eg, barrier-to-autointegration factor, germ cell-less, Btf), nesprins (proteins that act as molecular scaffolds), F-actin, and lamins. (medscape.com)
  • They bind to structural components (emerin, nesprin), chromatin components (histone), signal transduction molecules (protein kinase C), and several gene regulatory molecules. (medscape.com)
  • Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. (lu.se)
  • Smaug, a protein that helps to establish a morphogen gradient in Drosophila embryos by repressing the translation of nanos (nos) mRNA, binds to the 3' untranslated region (UTR) of nos mRNA via two similar hairpin structures. (embl.de)
  • Anteroposterior patterning in Drosophila melanogaster is dependent on the sequence-specific RNA-binding protein Smaug, which binds to and regulates the translation of nanos (nos) mRNA. (embl.de)
  • Lastly, mutations in the transmembrane protein 43 (TMEM43), also termed LUMA, which binds to emerin and SUN2, has also been reported to cause an EDMD phenotype in a few families. (medscape.com)
  • These are complexes that attach (bind) to proteins and then bind to the outer surface of the cell membrane to ensure that the protein is available on the cell surface when needed. (medlineplus.gov)
  • Thus, actin appears to be a bifunctional anchoring protein that is specific for the PKC epsilon isoform. (rupress.org)
  • Adapted with permission from (Siegel glycosylphosphatidylinositol-anchor into the cell membrane. (scienceexhibitions.org)
  • Although inhibitory postsynaptic sites lack PSDs, they also consist of complex protein matrices. (frontiersin.org)
  • This causes adaptor protein GRB2 to recruit SOS, a guanine nucleotide exchange factor, which then facilitates binding of GTP to Ras. (biolegend.com)
  • CD90 (Thy-1) is a GPI-anchored membrane glycoprotein of the Ig superfamily which is involved in signal transduction. (bdbiosciences.com)
  • Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase. (lu.se)
  • Scope includes mutations and abnormal protein expression. (cancerindex.org)
  • In 5 of 6 gene mutations that have been shown to cause EDMD, the affected protein is present in the LINC (linker of nucleoskeleton and cytoskeleton) complex. (medscape.com)
  • EDMD1 is caused by mutations in the EMD gene on the X chromosome that codes for the nuclear envelope protein emerin. (medscape.com)
  • Whatever the true mechanism, the discovery of mutations in several different nuclear membrane proteins that cause similar diseases will likely eventually lead to a better understanding of nuclear membrane physiology and the pathophysiology of diseases caused by mutations in these proteins. (medscape.com)
  • Exhaustive analysis of genetic mutations associated with protein S deficiency utilizing next-generation sequencing analysis]. (cdc.gov)
  • We found that a number of Tfh cells downmodulated BCL6 protein after their development, and we sought to compare the gene expression between BCL6-hi Tfh cells and BCL6-low Tfh cells. (gsea-msigdb.org)
  • Notably, expression of the kinase CaMKIV at day 3 was inversely correlated with later antibody titers. (gsea-msigdb.org)
  • Protein expression and purification 44 2.3.4. (fu-berlin.de)
  • This represents a new function for the SAM domain family, which is well characterized for mediating protein-protein interactions. (embl.de)
  • The capture is analogous to that seen for many DNA-binding proteins that have a weak non-specific affinity for DNA outside the canonical binding site, but different in that it involves (i) two proteins, and (ii) hydrophobic rather than electrostatic interactions. (kcl.ac.uk)
  • phosphodiesterases (PDEs) which break down cAMP, phosphatases which dephosphorylate downstream PKA targets and also other kinases (PKC and MAPK). (wikipedia.org)
  • Once the chain is formed, dolichol phosphate transports the oligosaccharide to the protein that needs to be glycosylated and attaches it to a specific site on the protein. (medlineplus.gov)
  • Dolichol phosphate is also needed for the formation of GPI anchors. (medlineplus.gov)
  • Without properly functioning dolichol kinase, dolichol phosphate is not produced and glycosylation cannot proceed normally. (medlineplus.gov)
  • However, in the mid 1990s, other proteins were also found to accumulate in the abnormal muscle fibers, and molecular genetic studies revealed several chromosomal loci. (medscape.com)
  • In addition, two other immunoreactive proteins of M(r) 109,000 (p109) and M(r) 26,000 (p26, representing the 'pro' domain of the precursor) were present in epididymal sperm. (elsevierpure.com)
  • Using a combination of cosedimentation, overlay, and direct binding assays, we demonstrate that filamentous actin is a principal anchoring protein for PKC epsilon within intact nerve endings. (rupress.org)
  • The unusual stability and direct nature of this physical interaction indicate that actin filaments represent a new class of PKC-binding protein. (rupress.org)
  • In addition, these proteins can also associate with claudin, occludin and F-actin, at tight junction stands, where they provide a linkage between the actin cytoskeleton and the tight junction. (thermofisher.com)
  • Tau is a microtubule-associated protein found predominantly in neuronal axons of the vertebrate brain. (biovendor.com)
  • Disordered scaffold proteins provide multivalent landing pads that, via a series of embedded Short Linear Motifs (SLiMs), bring together the components of a complex to orchestrate precise spatial and temporal regulation of cellular processes. (kcl.ac.uk)
  • Once established, this protein-protein interaction securely anchored PKC epsilon to the cytoskeletal matrix while also serving as a chaperone that maintained the kinase in a catalytically active conformation. (rupress.org)
  • The sterile alpha motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins [ ( PUBMED:9007998 ) ] involved in many biological processes. (embl.de)
  • CRISPRi genetic interaction analysis revealed Retro-2 activity resembles disruption of the transmembrane domain recognition complex (TRC) pathway, which mediates post-translational ER-targeting and insertion of tail-anchored (TA) proteins, including SNAREs required for retrograde transport. (elifesciences.org)
  • The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family. (cancerindex.org)
  • What does this gene/protein do? (cancerindex.org)
  • The protein encoded by this gene is an orphan G protein-coupled receptor whose ligand is unknown. (nih.gov)
  • Two Novel Variants in the Protein S Gene PROS1 Are Associated with Protein S Deficiency and Thrombophilia. (cdc.gov)
  • AZD8330 In contrast cancer cells express only high mannose-type structures (Holmes = to choose) are non-immunogenic (glyco)proteins that are able to specifically bind carbohydrate structures (http://goldbook.iupac.org). (scienceexhibitions.org)
  • At the same time, co-compartmentalization of enzymes or proteins that generate or terminate these second messenger metabolites, such as the phosphodiesterases (PDEs) which degrade cAMP and cGMP, with the relevant responsive kinases helps to optimise the precision and speed of response to second messenger signaling [ 10 ]. (biomedcentral.com)
  • These include proteins associated with the sarcolemma (see image below), proteins associated with the contractile apparatus (see image below), and various enzymes involved in muscle function. (medscape.com)
  • Widespread domain in signalling and nuclear proteins. (embl.de)
  • This complex includes nuclear membrane integral and associated proteins including emerin, lamin A/C, SUN1, SUN2, nesprin-1, and nesprin-2 that are proposed to form a mechanical link between the nucleoskeleton and cytoskeleton. (medscape.com)
  • This protein phosphatase isoform, which is highly expressed in testis, is present only in mammalian spermatozoa. (kent.edu)
  • Dudiki T, Joudeh N, Sinha N, Goswami S, Eisa A, Kline D, Vijayaraghavan S. The protein phosphatase isoform PP1γ1 substitutes for PP1γ2 to support spermatogenesis but not normal sperm function and fertility. (kent.edu)
  • Antibodies to this protein can be produced by patients with myasthenia gravis. (thermofisher.com)