The light chain subunits of clathrin.
The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
The heavy chain subunits of clathrin.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. Shortly after formation, however, the clathrin coat is removed and the vesicles are referred to as ENDOSOMES.
Specialized regions of the cell membrane composed of pits coated with a bristle covering made of the protein CLATHRIN. These pits are the entry route for macromolecules bound by cell surface receptors. The pits are then internalized into the cytoplasm to form the COATED VESICLES.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
Changes in the amounts of various chemicals (neurotransmitters, receptors, enzymes, and other metabolites) specific to the area of the central nervous system contained within the head. These are monitored over time, during sensory stimulation, or under different disease states.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule.
The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. Many myosin light chains that bind calcium are considered "calmodulin-like" proteins.
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
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.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
A subclass of clathrin assembly proteins that occur as monomers.

Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo. (1/30)

Clathrin heavy and light chains form triskelia, which assemble into polyhedral coats of membrane vesicles that mediate transport for endocytosis and organelle biogenesis. Light chain subunits regulate clathrin assembly in vitro by suppressing spontaneous self-assembly of the heavy chains. The residues that play this regulatory role are at the N terminus of a conserved 22-amino acid sequence that is shared by all vertebrate light chains. Here we show that these regulatory residues and others in the conserved sequence mediate light chain interaction with Hip1 and Hip1R. These related proteins were previously found to be enriched in clathrin-coated vesicles and to promote clathrin assembly in vitro. We demonstrate Hip1R binding preference for light chains associated with clathrin heavy chain and show that Hip1R stimulation of clathrin assembly in vitro is blocked by mutations in the conserved sequence of light chains that abolish interaction with Hip1 and Hip1R. In vivo overexpression of a fragment of clathrin light chain comprising the Hip1R-binding region affected cellular actin distribution. Together these results suggest that the roles of Hip1 and Hip1R in affecting clathrin assembly and actin distribution are mediated by their interaction with the conserved sequence of clathrin light chains.  (+info)

Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain. (2/30)

Huntingtin interacting protein 1 (HIP1) is a component of clathrin coats. We previously demonstrated that HIP1 promotes clathrin assembly through its central helical domain, which binds directly to clathrin light chains (CLCs). To better understand the relationship between CLC binding and clathrin assembly we sought to dissect this interaction. Using C-terminal deletion constructs of the HIP1 helical domain, we identified a region between residues 450 and 456 that is required for CLC binding. Within this region, point mutations showed the importance of residues Leu-451, Leu-452, and Arg-453. Mutants that fail to bind CLC are unable to promote clathrin assembly in vitro but still mediate HIP1 homodimerization and heterodimerization with the family member HIP12/HIP1R. Moreover, HIP1 binding to CLC is necessary for HIP1 targeting to clathrin-coated pits and clathrin-coated vesicles. Interestingly, HIP1 binds to a highly conserved region of CLC previously demonstrated to regulate clathrin assembly. These results suggest a role for HIP1/CLC interactions in the regulation of clathrin assembly.  (+info)

Clathrin heavy and light chain isoforms originated by independent mechanisms of gene duplication during chordate evolution. (3/30)

In humans, there are two isoforms each of clathrin heavy chain (CHC17 and CHC22) and light chain (LCa and LCb) subunits, all encoded by separate genes. CHC17 forms the ubiquitous clathrin-coated vesicles that mediate membrane traffic. CHC22 is implicated in specialized membrane organization in skeletal muscle. CHC17 is bound and regulated by LCa and LCb, whereas CHC22 does not functionally interact with either light chain. The imbalanced interactions between clathrin subunit isoforms suggest a distinct evolutionary history for each isoform pair. Phylogenetic and sequence analysis placed both heavy and light chain gene duplications during chordate evolution, 510-600 million years ago. Genes encoding CHC22 orthologues were found in several vertebrate species, with only a pseudogene present in mice. Multiple paralogons surrounding the CHC genes (CLTC and CLTD) were identified, evidence that genomic or large-scale gene duplication produced the two CHC isoforms. In contrast, clathrin light chain genes (CLTA and CLTB) apparently arose by localized duplication, within 1-11 million years of CHC gene duplication. Analysis of sequence divergence patterns suggested that structural features of the CHCs were maintained after gene duplication, but new interactions with regulatory proteins evolved for the CHC22 isoform. Thus, independent mechanisms of gene duplication expanded clathrin functions, concomitant with development of neuromuscular sophistication in chordates.  (+info)

Non-stoichiometric relationship between clathrin heavy and light chains revealed by quantitative comparative proteomics of clathrin-coated vesicles from brain and liver. (4/30)

We used tandem mass spectrometry with peptide counts to identify and to determine the relative levels of expression of abundant protein components of highly enriched clathrin-coated vesicles (CCVs) from rat liver. The stoichiometry of stable protein complexes including clathrin heavy chain and clathrin light chain dimers and adaptor protein (AP) heterotetramers was assessed. We detected a deficit of clathrin light chain compared with clathrin heavy chain in non-brain tissues, suggesting a level of regulation of clathrin cage formation specific to brain. The high ratio of AP-1 to AP-2 in liver CCVs is reversed compared with brain where there is more AP-2 than AP-1. Despite this, general endocytic cargo proteins were readily detected in liver but not in brain CCVs, consistent with the previous demonstration that a major function for brain CCVs is recycling synaptic vesicles. Finally we identified 21 CCV-associated proteins in liver not yet characterized in mammals. Our results further validate the peptide accounting approach, reveal new information on the properties of CCVs, and allow for the use of quantitative proteomics to compare abundant components of organelles under different experimental and pathological conditions.  (+info)

Membrane-associated STAT3 and PY-STAT3 in the cytoplasm. (5/30)

Signal transduction from the plasma membrane to the nucleus by STAT proteins is widely represented as exclusively a soluble cytosolic process. Using cell-fractionation methods, we observed that approximately 5% of cytoplasmic STAT3 was constitutively associated with the purified early endosome (EE) fraction in human Hep3B liver cells. By 15-30 min after interleukin-6 (IL-6) treatment, up to two-thirds of cytoplasmic Tyr-phosphorylated STAT3 can be associated with the purified early endosome fraction (Rab-5-, EEA1-, transferrin receptor-, and clathrin-positive fraction). Electron microscopy, immunofluorescence, and detergent dissection approaches confirmed the association of STAT3 and PY-STAT3 with early endosomes. STAT3 was constitutively associated with clathrin heavy chain in membrane and in the 1- to 2-MDa cytosolic complexes. The membrane association was dynamic in that, within 15 min of treatment with the vicinal-thiol cross-linker phenylarsine oxide, there was a dramatic increase in bulk STAT3 association with sedimentable membranes. The functional contribution of PY-STAT3 association with the endocytic pathway was evaluated in transient transfection assays using IL-6-inducible STAT3-reporter-luciferase constructs and selective regulators of this pathway. STAT3-transcriptional activation was inhibited by expression constructs for dominant negative dynamin K44A, epsin 2a, amphiphysin A1, and clathrin light chain but enhanced by that for the active dynamin species MxA. Taken together, these studies emphasize the contribution of the endocytic pathway to productive IL-6/STAT3 signaling.  (+info)

Clathrin light chain b is capable of affecting potently a major protein phosphatase from microtubules (MT-PP1). (6/30)

Clathrin light chain (CL) b purified from bovine brain postmicrotubule supernatant and identified by mass spectrometry potently inhibited a catalytic activity of a major protein phosphatase (PP) that was copurified with microtubules and recognized by antiPP1 antibodies. CLb similarly affected the catalytic subunit and holoenzyme of the PP, little inhibiting the activity of PP2A. Although the CLb from clathrin-coated vesicles was several hundredfold weaker than our purified CLb, the CLb in the postmicrotubule supernatant, independent of whether it was sedimentable or soluble, was as active as the purified CLb. Thus CLb may be a potent regulator of the PP.  (+info)

Calcyon, a novel partner of clathrin light chain, stimulates clathrin-mediated endocytosis. (7/30)

In the central nervous system, clathrin-mediated endocytosis is crucial for efficient synaptic transmission. Clathrin-coated vesicle assembly and disassembly is regulated by some 30 adaptor and accessory proteins, most of which interact with clathrin heavy chain. Using the calcyon cytosolic domain as bait, we isolated clathrin light chain in a yeast two-hybrid screen. The interaction domain was mapped to the heavy chain binding domain and C-terminal regions of light chain. Further, the addition of the calcyon C terminus stimulated clathrin self-assembly in a dose-dependent fashion. Calcyon, which is a single transmembrane protein predominantly expressed in brain, localized to vesicular compartments within pre- and postsynaptic structures. There was a high degree of overlap in the distribution of LC and calcyon in neuronal dendrites, spines, and cell bodies. Co-immunoprecipitation studies further suggested an association of calcyon with the clathrin-mediated endocytic machinery. Compared with controls, HEK293 cells overexpressing calcyon exhibited significantly enhanced transferrin uptake but equivalent levels of recycling. Conversely, transferrin uptake was largely abolished in neocortical neurons obtained from mice homozygous for a calcyon null allele, whereas recycling proceeded at wild type levels. Collectively, these data indicate a role for calcyon in clathrin-mediated endocytosis in brain.  (+info)

Novel function of clathrin light chain in promoting endocytic vesicle formation. (8/30)

Clathrin-mediated endocytosis is a major pathway for uptake of lipid and protein cargo at the plasma membrane. The lattices of clathrin-coated pits and vesicles are comprised of triskelions, each consisting of three oligomerized heavy chains (HC) bound by a light chain (LC). In addition to binding HC, LC interacts with members of the Hip1/R family of endocytic proteins, including the budding yeast homologue, Sla2p. Here, using in vivo analysis in yeast, we provide novel insight into the role of this interaction. We find that overexpression of LC partially restores endocytosis to cells lacking clathrin HC. This suppression is dependent on the Sla2p binding region of LC. Using live cell imaging techniques to visualize endocytic vesicle formation, we find that the N-terminal Sla2p binding region of LC promotes the progression of arrested Sla2p patches that form in the absence of HC. We propose that LC binding to Sla2p positively regulates Sla2p for efficient endocytic vesicle formation.  (+info)

Clathrin light chains are a type of protein that make up part of the clathrin coat, which is a lattice-like structure that helps form the outer shell of certain types of cellular structures called vesicles. These vesicles are involved in various cellular processes, such as endocytosis and intracellular trafficking.

Clathrin light chains combine with clathrin heavy chains to form triskelions, which are the building blocks of the clathrin lattice. There are two types of clathrin light chains, known as LCa and LCb, and they differ in their amino acid sequences and functions.

Clathrin light chains play a role in regulating the assembly and disassembly of the clathrin coat, and they have also been implicated in various signaling pathways within the cell. Mutations in clathrin light chain genes have been associated with certain diseases, such as neuromuscular disorders and cancer.

Clathrin is a type of protein that plays a crucial role in the formation of coated vesicles within cells. These vesicles are responsible for transporting materials between different cellular compartments, such as from the plasma membrane to the endoplasmic reticulum or Golgi apparatus. Clathrin molecules form a lattice-like structure that curves around the vesicle, providing stability and shape to the coated vesicle. This process is known as clathrin-mediated endocytosis.

The formation of clathrin-coated vesicles begins with the recruitment of clathrin proteins to specific sites on the membrane, where they assemble into a polygonal lattice structure. As more clathrin molecules join the assembly, the lattice curves and eventually pinches off from the membrane, forming a closed vesicle. The clathrin coat then disassembles, releasing the vesicle to continue with its intracellular transport mission.

Disruptions in clathrin-mediated endocytosis can lead to various cellular dysfunctions and diseases, including neurodegenerative disorders and certain types of cancer.

Clathrin Heavy Chains are the major structural components of clathrin coated vesicles, which are involved in intracellular trafficking and transport of proteins and lipids between different cellular compartments. These chains combine with light chains to form triskelions, a three-legged structure that polymerizes to form a cage-like lattice surrounding the vesicle membrane during the process of vesicle formation. The heavy chains are large polypeptides with a molecular weight of approximately 190 kDa and are subject to post-translational modifications such as phosphorylation, which can regulate their function in clathrin-mediated endocytosis.

Clathrin-coated vesicles are small, membrane-bound structures that play a crucial role in intracellular transport within eukaryotic cells. They are formed by the coating of the plasma membrane or the membranes of other organelles with a lattice-like structure made up of clathrin proteins.

The formation of clathrin-coated vesicles is initiated when adaptor proteins recognize and bind to specific signals on the cytoplasmic side of the membrane. These adaptor proteins then recruit clathrin molecules, which assemble into a cage-like structure that deforms the membrane into a spherical shape. The vesicle then pinches off from the membrane, enclosed in its clathrin coat.

Once formed, clathrin-coated vesicles can transport proteins and other molecules between different cellular compartments, such as from the plasma membrane to endosomes or from the Golgi apparatus to the endoplasmic reticulum. The clathrin coat is subsequently disassembled, allowing the vesicle to fuse with its target membrane and release its contents.

Defects in clathrin-coated vesicle function have been implicated in a variety of human diseases, including neurodegenerative disorders and certain forms of cancer.

Coated pits are specialized regions on the cell membrane that are involved in the process of endocytosis. They are called "coated" pits because they are covered or coated with a layer of proteins and clathrin molecules, which form a lattice-like structure that helps to shape and invaginate the membrane inward, forming a vesicle.

Coated pits play an important role in regulating cellular uptake of various substances, such as nutrients, hormones, and receptors. Once the coated pit has pinched off from the cell membrane, it becomes a coated vesicle, which can then fuse with other intracellular compartments to deliver its contents.

The formation of coated pits is a highly regulated process that involves the recruitment of specific proteins and adaptors to the site of endocytosis. Defects in this process have been implicated in various diseases, including neurodevelopmental disorders and cancer.

Endocytosis is the process by which cells absorb substances from their external environment by engulfing them in membrane-bound structures, resulting in the formation of intracellular vesicles. This mechanism allows cells to take up large molecules, such as proteins and lipids, as well as small particles, like bacteria and viruses. There are two main types of endocytosis: phagocytosis (cell eating) and pinocytosis (cell drinking). Phagocytosis involves the engulfment of solid particles, while pinocytosis deals with the uptake of fluids and dissolved substances. Other specialized forms of endocytosis include receptor-mediated endocytosis and caveolae-mediated endocytosis, which allow for the specific internalization of molecules through the interaction with cell surface receptors.

Brain chemistry refers to the chemical processes that occur within the brain, particularly those involving neurotransmitters, neuromodulators, and neuropeptides. These chemicals are responsible for transmitting signals between neurons (nerve cells) in the brain, allowing for various cognitive, emotional, and physical functions.

Neurotransmitters are chemical messengers that transmit signals across the synapse (the tiny gap between two neurons). Examples of neurotransmitters include dopamine, serotonin, norepinephrine, GABA (gamma-aminobutyric acid), and glutamate. Each neurotransmitter has a specific role in brain function, such as regulating mood, motivation, attention, memory, and movement.

Neuromodulators are chemicals that modify the effects of neurotransmitters on neurons. They can enhance or inhibit the transmission of signals between neurons, thereby modulating brain activity. Examples of neuromodulators include acetylcholine, histamine, and substance P.

Neuropeptides are small protein-like molecules that act as neurotransmitters or neuromodulators. They play a role in various physiological functions, such as pain perception, stress response, and reward processing. Examples of neuropeptides include endorphins, enkephalins, and oxytocin.

Abnormalities in brain chemistry can lead to various neurological and psychiatric conditions, such as depression, anxiety disorders, schizophrenia, Parkinson's disease, and Alzheimer's disease. Understanding brain chemistry is crucial for developing effective treatments for these conditions.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Immunoglobulin light chains are the smaller protein subunits of an immunoglobulin, also known as an antibody. They are composed of two polypeptide chains, called kappa (κ) and lambda (λ), which are produced by B cells during the immune response. Each immunoglobulin molecule contains either two kappa or two lambda light chains, in association with two heavy chains.

Light chains play a crucial role in the antigen-binding site of an antibody, where they contribute to the specificity and affinity of the interaction between the antibody and its target antigen. In addition to their role in immune function, abnormal production or accumulation of light chains can lead to various diseases, such as multiple myeloma and amyloidosis.

Myosin light chains are regulatory proteins that bind to the myosin head region of myosin molecules, which are involved in muscle contraction. There are two types of myosin light chains, essential and regulatory, that have different functions. The essential light chains are necessary for the assembly and stability of the myosin filaments, while the regulatory light chains control the calcium-sensitive activation of the myosin ATPase activity during muscle contraction. Phosphorylation of the regulatory light chains plays a critical role in regulating muscle contraction and relaxation.

In the context of medical terminology, "light" doesn't have a specific or standardized definition on its own. However, it can be used in various medical terms and phrases. For example, it could refer to:

1. Visible light: The range of electromagnetic radiation that can be detected by the human eye, typically between wavelengths of 400-700 nanometers. This is relevant in fields such as ophthalmology and optometry.
2. Therapeutic use of light: In some therapies, light is used to treat certain conditions. An example is phototherapy, which uses various wavelengths of ultraviolet (UV) or visible light for conditions like newborn jaundice, skin disorders, or seasonal affective disorder.
3. Light anesthesia: A state of reduced consciousness in which the patient remains responsive to verbal commands and physical stimulation. This is different from general anesthesia where the patient is completely unconscious.
4. Pain relief using light: Certain devices like transcutaneous electrical nerve stimulation (TENS) units have a 'light' setting, indicating lower intensity or frequency of electrical impulses used for pain management.

Without more context, it's hard to provide a precise medical definition of 'light'.

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.

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.

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.

Fluorescence microscopy is a type of microscopy that uses fluorescent dyes or proteins to highlight and visualize specific components within a sample. In this technique, the sample is illuminated with high-energy light, typically ultraviolet (UV) or blue light, which excites the fluorescent molecules causing them to emit lower-energy, longer-wavelength light, usually visible light in the form of various colors. This emitted light is then collected by the microscope and detected to produce an image.

Fluorescence microscopy has several advantages over traditional brightfield microscopy, including the ability to visualize specific structures or molecules within a complex sample, increased sensitivity, and the potential for quantitative analysis. It is widely used in various fields of biology and medicine, such as cell biology, neuroscience, and pathology, to study the structure, function, and interactions of cells and proteins.

There are several types of fluorescence microscopy techniques, including widefield fluorescence microscopy, confocal microscopy, two-photon microscopy, and total internal reflection fluorescence (TIRF) microscopy, each with its own strengths and limitations. These techniques can provide valuable insights into the behavior of cells and proteins in health and disease.

Monomeric Clathrin Assembly Proteins (also known as Clathrin Terminal Domain Proteins or CTD proteins) refer to a group of proteins that play a crucial role in the assembly and disassembly of clathrin-coated vesicles, which are involved in intracellular trafficking processes such as endocytosis and recycling of membrane receptors.

Clathrin is a triskelion-shaped protein made up of three heavy chains and three light chains. The monomeric clathrin assembly proteins, including CTD-associated proteins (CAPs) and serine kinases such as Clathrin Kinase (CLK), interact with the terminal domains of clathrin's heavy chains to regulate the formation and stability of clathrin lattices.

These proteins facilitate the self-assembly of clathrin molecules into polyhedral cages, which then deform the membrane and form vesicles that bud off from the plasma membrane or intracellular organelles. The monomeric clathrin assembly proteins also play a role in regulating the disassembly of these structures during the uncoating process, allowing for the recycling of clathrin molecules and the release of cargo.

In summary, Monomeric Clathrin Assembly Proteins are essential components of the clathrin-mediated trafficking pathway, facilitating the formation, stability, and disassembly of clathrin-coated vesicles.

Identification of a novel interaction with clathrin light chain". J. Biol. Chem. 277 (22): 19897-904. doi:10.1074/jbc. ... 2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8". Proteomics. 4 (2): 339-46. doi: ... 2002). "HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. ...
There are two forms of clathrin light chains, designated a and b. The main clathrin heavy chain, located on chromosome 17 in ... The three heavy chains provide the structural backbone of the clathrin lattice, and the three light chains are thought to ... It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they ... A second clathrin heavy chain gene, on chromosome 22, is expressed in muscle. Clathrin heavy chain is often described as a leg ...
Clathrin, light chain B is a protein in humans that is encoded by the CLTB gene. Clathrin is a large, soluble protein composed ... "Entrez Gene: Clathrin, light chain B". Retrieved 2013-06-05. v t e (Articles with short description, Short description matches ... This gene encodes one of two clathrin light chain proteins which are believed to function as regulatory elements. Alternative ... of heavy and light chains. It functions as the main structural component of the lattice-type cytoplasmic face of coated pits ...
"Localization of clathrin light-chain sequences mediating heavy-chain binding and coated vesicle diversity". Nature. 326 (6109 ... "Clathrin light chains' role in selective endocytosis influences antibody isotype switching". Proceedings of the National ... "A role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism". Science. 324 (5931): 1192-1196. Bibcode:2009Sci ... She is known for her work on clathrin and its role in the function of the immune system. She is a professor of cell biology and ...
Xiao J, Dai R, Negyessy L, Bergson C (June 2006). "Calcyon, a novel partner of clathrin light chain, stimulates clathrin- ...
HIP1's non-pathological activity includes clathrin assembly via interaction with clathrin light chains. HIP1 is the human ... regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain". The Journal of ... Actin binding by Hip-1 is altered depending on whether clathrin is also bound to Hip-1. HIP1 has also been found to be ...
"Chromosomal location and some structural features of human clathrin light-chain genes (CLTA and CLTB)". Genomics. 24 (3): 440-4 ... The enzyme is used in DNA repair, where it hydrolysis the oxidized purines and prevents their addition onto the DNA chain. ... During DNA repair, the enzyme hydrolyses oxidized purines and prevents their addition onto the DNA chain. As such it has ...
"Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3". J. Biol. Chem ... The basic subunit of the clathrin coat is composed of three heavy chains and three light chains. CLTC has been shown to ... Clathrin heavy chain 1 is a protein that in humans is encoded by the CLTC gene. Clathrin is a major protein component of the ... "Entrez Gene: CLTC clathrin, heavy chain (Hc)". Tebar, F; Bohlander S K; Sorkin A (Aug 1999). "Clathrin assembly lymphoid ...
October 2019). "Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension". ... "Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis". The EMBO Journal. 20 (14 ... Myosin-VI's Met-Ile-Sec bonding interactions are limited to the myosin-VI long isoform but interact with clathrin in ... MYO6 has been shown to interact with GIPC1, DAB2., ubiquitin, and clathrin. Myosin VI, being a motor protein, focuses its ...
... binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis". Cell. 62 (5): 875-87. doi: ... Another function of Hsc70 is as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane ... It works with auxilin to remove clathrin from coated vesicles. In neurons, synaptojanin is also an important protein involved ...
Dhingra A, Alexander D, Reyes-Reveles J, Sharp R, Boesze-Battaglia K (2018). "Microtubule-Associated Protein 1 Light Chain 3 ( ... These AP2 aggregates interact with individual clathrin proteins by their β-active sites, orienting them into the clathrin " ... which would serve as an important receptor group for microtubule-associated protein 1 light chain 3 (LC3). LC3 has an important ... of the clathrin trimer. AP2 facilitates the assembly of clathrin lattices when endocytosis needs to occur, by aggregating ...
... clathrin heavy chains MeSH D12.776.543.990.200.750 - clathrin light chains MeSH D12.776.543.990.300.150 - ADP-ribosylation ... cd98 heavy chain MeSH D12.776.543.585.200.374.750.500.500 - antigens, cd98 light chains MeSH D12.776.543.585.200.500 - amino ... cd98 heavy chain MeSH D12.776.543.585.200.500.500.500.500 - antigens, cd98 light chains MeSH D12.776.543.585.200.500.500.500. ... integrin alpha chains MeSH D12.776.543.750.705.408.100.100 - antigens, cd11a MeSH D12.776.543.750.705.408.100.150 - antigens, ...
Mann SS, Hammarback JA (1994). "Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B ... "Interactions between adaptor protein-1 of the clathrin coat and microtubules via type 1a microtubule-associated proteins". J. ... polypeptide that presumably undergoes proteolytic processing to generate the final MAP1A heavy chain and LC2 light chain. ... light chains determine distinct functional properties". J. Neurosci. 22 (6): 2106-14. doi:10.1523/JNEUROSCI.22-06-02106.2002. ...
... kD protein called clathrin light chain (CLC), forming three-legged trimers called triskelions. Vesicles selectively concentrate ... The main scaffold component of clathrin coat is the 190-kD protein called clathrin heavy chain (CHC), which is associated with ... Clathrin-coated vesicles (CCVs) are found in virtually all cells and form domains of the plasma membrane termed clathrin-coated ... Clathrin-mediated endocytosis is the only pathway dependent on both clathrin and dynamin. The endocytic pathway of mammalian ...
I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of ... This article deals with protein targeting in eukaryotes unless specified otherwise Bulk flow COPI COPII Clathrin LocDB PSORTdb ... The amino acid chain of transmembrane proteins, which often are transmembrane receptors, passes through a membrane one or ... Once in the lumen the polypeptide chain can be folded properly. This process only occurs in unfolded proteins located in the ...
"Light-dependent inhibition of clathrin-mediated endocytosis in yeast": 2021.04.01.432428. doi:10.1101/2021.04.01.432428. S2CID ... in the side chains or in the backbone of peptide templates to get the photo-controlled peptides, which can reversibly change ... "Light-Regulated Stapled Peptides to Inhibit Protein-Protein Interactions Involved in Clathrin-Mediated Endocytosis". Angewandte ... light. Photoswitchable peptides to inhibit protein-protein interactions in a light-controlled manner have been developed and ...
The N-terminus (one end) of a polypeptide chain (i.e., a protein) contains a few amino acids that work as an address tag, which ... The ER was observed by light microscopy by Garnier in 1897, who coined the term ergastoplasm. The lacy membranes of the ... either secreted constitutively with no tag or secreted in a regulatory manner involving clathrin and paired basic amino acids ... to the side-chain nitrogen of Asn. In most cells the smooth endoplasmic reticulum (abbreviated SER) is scarce. Instead there ...
... clathrin adaptor molecules); thus, the arrestin here acts as a scaffold assembling the components needed for clathrin-mediated ... Cyclic AMP-dependent protein kinases (protein kinase A) are activated by the signal chain coming from the G protein (that was ... This mechanism is used, for example, with rhodopsin in retina cells to compensate for exposure to bright light. In many cases, ... which in turn recruits another protein called clathrin. If enough receptors in the local area recruit clathrin in this manner, ...
Hemoglobin Myoglobin Angiotensin II Insulin Leptin Prolactin Epidermal Growth Factor Cathepsin B Immunoglobulin light chains ... Once internalized, the endosomes release their clathrin coats and fuse with a dense subapical network of tubules to recycle ... LRP2 has a NPXY motif that is the binding site for Dab2 to initiate clathrin-mediated endocytosis. LRP2 forms a homodimer that ... where Dab2 binds to the cytoplasmic tails of both LRP2 and CUBAM to initiate clathrin-coated endocytosis. ...
The structure of Dynein consists of A Stem Containing A region that binds to dynactin Intermediate/light chains that will ... Dynamin is responsible for the separation of clathrin buds from the plasma membrane. GTP is used. Rotary motors: FoF1-ATP ...
... and translocation of the light chain into the cytosol. The light chain has zinc-dependent endopeptidase or more specifically ... clathrin-coated, single-membrane vesicles containing Atg16L, the v-SNARE VAMP7, and its partner t-SNAREs: Syntaxin-7, Syntaxin- ... Finally, after the light chain of BoNT is brought into the cytosol of the targeted neuron, it is released from the heavy chain ... The light chain is released from the heavy chain by the reduction of the disulfide bond holding the two together. The reduction ...
Binding to αv integrin results in endocytosis of the virus particle via clathrin-coated pits. Attachment to αV integrin ... Such MR was demonstrated for adenovirus 12 after virions were irradiated with UV light and allowed to undergo multiple ... In the laboratory, adenovirus can be identified with antigen detection, polymerase chain reaction (PCR), virus isolation and ... "Multiplicity reactivation of human adenovirus type 12 and simian virus 40 irradiated by ultraviolet light". Virology. 45 (2): ...
Lo KW, Kogoy JM, Pfister KK (April 2007). "The DYNLT3 light chain directly links cytoplasmic dynein to a spindle checkpoint ... Cayrol C, Cougoule C, Wright M (November 2002). "The beta2-adaptin clathrin adaptor interacts with the mitotic checkpoint ...
Clathrin is involved in cellular endocytosis and is sequestrated by specific signaling molecules. Clathrin can attach to ... On the other hand, lipids with smaller acyl chain area to polar head group area ratio tend to curve positively, in other words ... Polishchuk RS, Polishchuk EV, Marra P, Alberti S, Buccione R, Luini A, Mironov AA (January 2000). "Correlative light-electron ... Clathrin binds to its receptors that are present in the membrane. The overall shape of a cell is mostly determined by its ...
Fausser JL, Ungewickell E, Ruch JV, Lesot H (October 1993). "Interaction of vinculin with the clathrin heavy chain". Journal of ... The recent discovery of the 3D structure sheds light on how this protein tailors its shape to perform a variety of functions. ...
... which activates myosin II directly by phosphorylation of the myosin light chain and also inhibits myosin phosphatase by ... large amounts of membrane material are removed via clathrin-mediated endocytosis [7] Eventually, the edges of the cell plate ... a striking process that is clearly visible through a light microscope. The cytokinetic furrow ingresses until a midbody ...
From outside the LMB, the parent MRC ensured that the quinquennial assessment had a light touch: only a brief explanation of ... Barbara Pearse discovered the major components of clathrin-coated vesicles, structures formed during endocytosis, and a low ... J. A. Steitz, (1969) "Polypetide Chain Initiation: Nucleotide Sequences of the Three Ribosomal Binding Sites in Bacteriophage ...
MLK2 is myosin light chain kinase 2 The b2 adaptin of the AP2 complex Calcium-dependent activator protein for secretion (CADPS ... clathrin and tubulin". Biochem. J. 363 (Pt 3): 599-608. doi:10.1042/0264-6021:3630599. PMC 1222513. PMID 11964161. O'Callaghan ...
Tubulin Acetylation Protein Isoform Post-translational modification Microtubules Clathrin Portal: Biology (EC 2.3.1, Enzymes of ... Isoform 4 Isoform 4 is different to the canonical sequence as the sequence of amino acids 323-333 from the canonical chain ( ... it might play an important paper in the intracilial transport of signal proteins during light-sensing signaling in ... or the clathrin coated-pit in the membrane. This is closely related to one of its main functions which is the catalysis of ...
Reverse transcription polymerase chain reaction studies have shown expression of the a4 subunit in the intercalated cell of the ... A relatively new technique called ancestral gene resurrection has shed new light on the evolutionary history of the V-ATPase. ... Forgac M (January 1999). "The vacuolar H+-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione". ...
Identification of a novel interaction with clathrin light chain". J. Biol. Chem. 277 (22): 19897-904. doi:10.1074/jbc. ... 2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8". Proteomics. 4 (2): 339-46. doi: ... 2002). "HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. ...
clathrin light chain B [Source:HGNC Sy.... COL4A3. 1285. COL4A3. collagen type IV alpha 3 chain [Source.... ...
Clathrin Light Chain-1; EPG-3, Ectopic P Granules-3; EPG-6, Ectopic P Granules-6; LGG-1, LC3, GABARAP and GATE-16 family-1; ... microtubule-associated protein 1 light chain 3; PD, Parkinson disease; PtdIns3P, phosphatidylinositol-3-phosphate; PtdIns(4,5) ... Clathrin is also an important ALR regulator implicated in autolysosome tubule formation and release. In C. elegans we found ... Clathrin is also an important ALR regulator implicated in autolysosome tubule formation and release. In C. elegans we found ...
pEGFP-GFP11-Clathrin light chain * pHRm-NLS-dCas9-GFP11x7-NLS How was your experience today? ...
... light_chain 1 XM0045195921 IPR013015 DOMAIN:Laminin_IV_B 1 XM0045313792 IPR034884 DOMAIN:Cytochrome_c_oxidase_VIc/VIIs 2 ... Clathrin_H-chain_propeller_rpt 1 XM0045235872 IPR013969 FAMILY:Oligosacch_biosynth_Alg14 1 XM0045239062 IPR022031 DOMAIN:Rif1_N ... light_intermed_chain 1 XM0045199732 IPR030348 FAMILY:ATP8B4 1 XM0123052531 IPR018121 DOMAIN:7-in-absentia-prot_TRAF-dom 2 ... Clathrin_L-chain 1 XM0045221942 IPR041207 DOMAIN:NUB1_ubiquitin-like_dom 1 XM0045238912 IPR015221 FAMILY:Urm1 1 XM0045245072 ...
Clathrin Light Chain Binding. Biological Process. *Nuclear-transcribed MRNA Catabolic Process, Nonsense-mediated Decay ...
... to the plasma membrane leading to activation of myosin light-chain kinase (MLCK), which triggers the release of MVs [67,69]. ... Internalization of EVs by recipient cells occurs by various mechanisms of endocytosis including clathrin-dependent and clathrin ... Tian, T.; Zhu, Y.-L.; Zhou, Y.-Y.; Liang, G.-F.; Wang, Y.-Y.; Hu, F.-H.; Xiao, Z.-D. Exosome uptake through clathrin-mediated ... Chu, J.J.H.; Ng, M.L. Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway. J. Virol. 2004 ...
... activates nuclear factor kappa light-chain enhancer of activated B cells (NF-B) and mitogen-activated protein kinase (MAPK) ... specifically clathrin-mediated endocytosis, caveolae-mediated endocytosis, macropinocytosis, and phagocytosis (7, 8). However, ...
2007) and is light from the cytosolic transrepression. The syndrome of PI5P in the lysine lacks associated rather because of ... Although Clathrin-mediated endocytosys causes to have the primary download hegels family, it promotes digital whether it not ... IRAK-1 genomes were that tetramers to EMILIN can be the wave of metabolic chain death( Bressan et al. EMILIN1 occurs formed ... chains known with, and becomes of, download hegels idea of freedom oxford philosophical monographs 1999 Carbohydrate in the ...
... and then ERK phosphorylates and activates myosin light-chain kinase (MLCK) which is an important regulator of actin ... which are organized by clathrin into specialized endosomal subdomains [23]. Then, direct interaction between ESCRT-0 and TSG101 ... G. van Niel, G. DAngelo, and G. Raposo, "Shedding light on the cell biology of extracellular vesicles," Nature Reviews ...
CNF-1 also induced displacement of a TJ-associated pool of phosphorylated myosin light chain (p-MLC), which is normally also ... We found that LNPs enter cells by both constitutive and inducible pathways in a cell type-specific manner using clathrin- ... Correlative Light and Electron Microscopy of Early Caenorhabditis elegans Embryos in Mitosis.. In: Cellular electron microscopy ... Long-chain fatty acid uptake into adipocytes depends on lipid raft function.. Biochemistry, 43(14) 4179-4187 (2004) Abstract. ...
Both the heavy chains are linked together by two disulphide bridges at the hinge region. Likewise, each light chain is linked ... Phagocytosis, macropinocytosis, clathrin and caveolae mediated endocytosis have all been implicated in the energy dependent ... Furthermore, the chain transfer reactions are responsible for transfer the active radical between polymer chains or another ... Propagation involves the growth of polymer chains by monomer addition to the end chain radical. The concluding step of ...
... both of which are known to prevent clathrin disassembly and receptor recycling to the plasmic membrane during clathrin-mediated ... complex IC50(dark)/μM IC50(light)/μM PIb. 1 ,200 ,200 c. 1a 66.1 ± 4.8 63.5 ± 2.7 1.0. 1b ,200 ,200 c. 2 ,200 ,200 c. 2a 60.4 ... The PEG complex 3b was used to investigate the impact of a hydrophilic chain on the cell internalization and intracellular ... Importantly, the attachment of a large POSS cage or a long PEG chain to cyclometalated iridium(III) complexes rendered them ...
... functioning as the key regulator of the late stages of clathrin-coated vesicle budding. It is specifically targeted to clathrin ... spectrin beta-chain, syntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1. ... point mutations within the Btk PH domain which cause XLA can be classified as either structural or functional in the light of ... is distal to the region of the molecule where the N and C termini reside and where SH3 inserts into the alpha-spectrin chain. ...
Clathrin-Mediated Recycling Of ZG Membranes To The Golgi Complex - Following removal of the GP2/PG skeletal matrix from their ... In the light of this idea, he reasons, devises an experiment, imagines and brings to pass its material conditions. From this ... PH-dependent formation of tetrameric GP2 complexes in the TGN would allow for multivalent association of proteoglycan chains, ... Inhibition of clathrin processes would prevent vesicular budding in granule membranes. This hypothesis is consistent with the ...
The ER was observed by light microscopy by Garnier in 1897, who coined the term ergastoplasm.[2][3] The lacy membranes of the ... The N-terminus (one end) of a polypeptide chain (i.e., a protein) contains a few amino acids that work as an address tag, which ... either secreted constitutively with no tag or secreted in a regulatory manner involving clathrin and paired basic amino acids ... to the side-chain nitrogen of Asn. ...
Clathrin.pdf. The clathrin heavy chain repeat is composed of the main chain units of its peptides joined as 32-chain linked ... The chapter LIGHT excerpted from Octahedron1stEd.pdf.. LTriplets.pdf. Shows thirteen ways in which one L-triplet can join with ... Shows how strands of a pleated sheet can be joined by short lengths of main chain units to form a single chain. The strand ... Shows how S-shaped sheet forming chains can have multilength 32-strands between its beta180-strands. A fibroin-like chain which ...
This study sheds light on the mechanisms involved in α-syn toxicity found in Parkinsons disease and other alpha- ... Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J Biol Chem. 2001; 276:41958- ... Yeast Gga coat proteins function with clathrin in Golgi to endosome transport. Mol Biol Cell. 2001; 12:1885-96. https://doi.org ...
These findings highlight the importance of comparative neurological assessment in mouse models of disease and shed light on key ... Neurotrophins redirect p75NTR from a clathrin-independent to a clathrin-dependent endocytic pathway coupled to axonal transport ... These findings highlight the importance of comparative neurological assessment in mouse models of disease and shed light on key ... transients through Cav2.2 calcium channels in motoneurons corresponds to F-actin assembly and growth cone formation on β2-chain ...
Microtuble-associated protein 1 light chain 3 (LC3) is a mammalian protein specifically associated with autophagosome membrane ... 2012) Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation. Nat Cell Biol 14:924-934, ... In light of this, we began our inquiry into the contribution of these ARFs to mutant SOD toxicity. The ARF6 mutant allele ... In light of the observation that secinH3 was neuroprotective, reduced ER stress, and stimulated autophagic flux, we next ...
Myosin regulatory light chain phosphorylation by ROCK (Homo sapiens) * p-T19,S20-MRLC-smooth muscle/non-muscle myosin II [ ... PolyUb-CFTR [clathrin-coated endocytic vesicle membrane] (R-HSA-8869104) * PolyUb-CFTR [plasma membrane] (R-HSA-8867595) ... Myosin regulatory light chain phosphorylation by ROCK (Homo sapiens) * p-T19,S20-MRLC-smooth muscle/non-muscle myosin II [ ... Phosphorylated smooth muscle/non-muscle myosin 2 regulatory light chains [cytosol] (Homo sapiens) * p-T19,S20-MYL9 [cytosol] ( ...
This protein is composed of a chain of 104 amino acids with an iron-containing heme molecule. It is often used for protein ... X-ray Scattering Shines Light on Protein Folding​ View. : 9666 Date. : 2020-07-09 Writer. : PR Office ... research KAIST research team develops clathrin assembly for targeted protein delivery to cancer cells In order to effectively ... The researchers placed the protein in a solution and shined ultraviolet light on it. This process provides electrons to ...
Model cargos, which are endocytosed from the basolateral PM via clathrin-dependent endocytosis CDE or clathrin-independent ... Big Space Benjamin fortnite aim lock free Berkshire Beige - Here, light fixtures, rugs and arched opening mark the space to ... Introduction of a side chain to octanoic acid increased suppression of PTZ-induced epileptiform discharges when branched on the ...
demonstrated a significantly greater number of bacteria (via polymerase chain reaction identification of total bacterial 16S ... Upon binding of brentuximab vedotin to CD30, the receptor-antibody complex undergoes clathrin mediated endocytosis and ... In light of mounting data supporting this association, the Food and Drug Administration (FDA) released a safety communication ... most often of the axillary chain, portending a worse prognosis [43]. ...
chain role is selective for beta function when redox is M1, while hot PDH actin dissociates mediated to proceed both ATP and ... download Virgil, Aeneid 2: growth over the sensitive sulfate light-strand of a polymerase is the most many polymerase of ... activation of clathrin-dependent symporter factors, IL-1 transcription to include protein, vascular %, and the HSP90 cytosol ... IGFBP3 carries a NOTCH2 size of TP53 that may play as a duct for a mitochondrial chain complementation TMEM219( Buckbinder et ...
HIV-1 viral infectivity factor interacts with microtubule-associated light chain 3 and inhibits autophagy. ... We found that Tat is then endocytosed using the clathrin/AP-2 pathway (Vendeville et al, 2004). Once in endosomes, low pH ...
"In stark contrast to the products mentioned above, collagen (VI) α1 chain precursor protein is decreased in fetal DS brain ( ... Even after the principles of epigenetics came to light, it was believed that methylation marks and other epigenetic changes to ... 2002). It modulates synaptic transmission and plays a role in clathrin-mediated synaptic vesicle endocytosis and signalling. ... The implications of the epigenetic revolution are even more profound in light of recent evidence that epigenetic changes made ...
  • Clathrin is a protein that plays a major role in the formation of coated vesicles. (wikipedia.org)
  • Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. (wikipedia.org)
  • Clathrin performs critical roles in shaping rounded vesicles in the cytoplasm for intracellular trafficking. (wikipedia.org)
  • Clathrin-coated vesicles (CCVs) selectively sort cargo at the cell membrane, trans-Golgi network, and endosomal compartments for multiple membrane traffic pathways. (wikipedia.org)
  • Epsin also recruits clathrin to membranes and promotes its polymerization, and can help deform the membrane, and thus clathrin-coated vesicles can bud. (wikipedia.org)
  • In non-dividing cells, the formation of clathrin-coated vesicles occurs continuously. (wikipedia.org)
  • Its matrix is to as prevent and require the pre-leukemic humans of several vesicles and include drug chains to act Affected cytosol, non-canonical target energy about their elements biologically in the kinase. (erik-mill.de)
  • In a cell, clathrin triskelion in the cytoplasm binds to an adaptor protein that has bound membrane, linking one of its three feet to the membrane at a time. (wikipedia.org)
  • TLR4, the PRR that specifically Haloxon recognizes lipopolysaccharide (LPS) of Gram-negative bacteria, activates nuclear factor kappa light-chain enhancer of activated B cells (NF-B) and mitogen-activated protein kinase (MAPK) through myeloid differentiation factor 88 (MyD88) to induce the expression of proinflammatory cytokines (2, 3). (monossabios.com)
  • Cytoskeletal proteins such as dynamin (see IPR001401 ), Caenorhabditis elegans kinesin-like protein unc-104 (see IPR001752 ), spectrin beta-chain, syntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1. (embl.de)
  • This protein is composed of a chain of 104 amino acids with an iron-containing heme molecule. (kaist.ac.kr)
  • The researchers placed the protein in a solution and shined ultraviolet light on it. (kaist.ac.kr)
  • The concluding step of termination proceeds with a combination of coupling and disproportionation of two end chain radicals to produce inactive polymers. (ukdiss.com)
  • These findings highlight the importance of comparative neurological assessment in mouse models of disease and shed light on key proposed neuropathogenic mechanisms in GARS1 -linked neuropathy. (frontiersin.org)
  • This was originally determined from the structure of the proximal leg domain that identified and is composed of a smaller structural module referred to as clathrin heavy chain repeat motifs. (wikipedia.org)
  • The clathrin heavy chain repeat is composed of the main chain units of its peptides joined as 32-chain linked alpha helixes. (robertwilliamwhitby.com)
  • It recruits clathrin to membranes and also promotes its polymerization. (wikipedia.org)
  • Furthermore, the chain transfer reactions are responsible for transfer the active radical between polymer chains or another species within the polymerization system. (ukdiss.com)
  • In addition, initiation is usually slower than propagation, which suggests that as the polymerization proceeds, some chains have grown significantly while others are still initiating ( Colombani, 1997 ). (ukdiss.com)
  • The main clathrin heavy chain, located on chromosome 17 in humans, is found in all cells. (wikipedia.org)
  • Clathrin has another function aside from the coating of organelles. (wikipedia.org)
  • Proton leakage from organelles is a common signal for noncanonical light chain 3B (LC3B) lipidation and inflammasome activation, processes induced upon stimulator of interferon gene (STING) activation. (tcdb.org)
  • Shows how 32-strands can form sheets in which the strands are anti-parallel and the link between adjacent strands is provided by a single peptide main chain unit. (robertwilliamwhitby.com)
  • Propagation involves the growth of polymer chains by monomer addition to the end chain radical. (ukdiss.com)
  • download Virgil, Aeneid 2: growth over the sensitive sulfate light-strand of a polymerase is the most many polymerase of ubiquinone MAP3. (evakoch.com)
  • Conformational changes in endocytic proteins are regulators of clathrin-mediated endocytosis. (nih.gov)
  • Three clathrin heavy chains associated with clathrin light chains (CLC) assemble into triskelia that link into a geometric lattice that curves to drive endocytosis. (nih.gov)
  • The primary retrieval mechanism in eukaryotic cells is clathrin-mediated endocytosis (CME). (nih.gov)
  • [ 28 ] This results in virus endocytosis, primarily via the formation of clathrin-coated vesicles regulated by dynamin. (medscape.com)
  • This then triggers clathrin-mediated endocytosis and partial virus disassembly. (medscape.com)
  • The migration of ATP7A appears to involve amino acid sequences in the carboxyl terminus, utilizing both clathrin-dependent and clathrin-independent endocytosis. (medscape.com)
  • The most studied and best understood type of endocytosis is clathrin-mediated endocytosis in the selective uptake of specific receptors and ligands into cells. (nih.gov)
  • By contrast, very little is known about the various clathrin-independent forms of endocytosis. (nih.gov)
  • We began to characterize a novel clathrin-independent endocytosis pathway through our studies on Arf6, a low- molecular-weight GTP-binding protein (GTPase). (nih.gov)
  • The short cytoplasmic domain binds the clathrin adaptors for endocytosis. (ossn.cr)
  • The canonical pathway has been suggested to occur via Leucine-rich repeat-containing G-protein coupled receptors 5 and 6 LGR5 and LGR6 in hacks pubg clathrin endocytosis-dependent fashion 14, 15. (lasalona.es)
  • These findings indicate that AP-3-clathrin association is dispensable for endosomal AP-3 vesicle budding and suggest that endosomal AP-3-clathrin interactions differ from those by which AP-1 and AP-2 adaptors productively engage clathrin in vesicle biogenesis. (nih.gov)
  • Then, as an independent investigator, my colleagues and I began studying Arf6 and found that this Arf localizes to the plasma membrane and to endosomal membranes that are distinct in protein and lipid composition from those endosomes derived from the clathrin-mediated endocytic pathway. (nih.gov)
  • We find that AP-3 interacts and colocalizes with endogenous and recombinant FKBP chimeric clathrin polypeptides in PC12-cell endosomes. (nih.gov)
  • Chemical-genetic disruption of clathrin function spares adaptor complex 3-dependent endosome vesicle biogenesis. (nih.gov)
  • A role for clathrin in AP-3-dependent vesicle biogenesis has been inferred from biochemical interactions and colocalization between this adaptor and clathrin. (nih.gov)
  • We comprehensively explore the role of clathrin in AP-3-dependent vesicle budding, using rapid chemical-genetic perturbation of clathrin function with a clathrin light chain-FKBP chimera oligomerizable by the drug AP20187. (nih.gov)
  • AP-3 cofractionates with clathrin-coated vesicle fractions isolated from PC12 cells even after clathrin function is acutely inhibited by AP20187. (nih.gov)
  • AP-3 vesicle formation continued, however, after brefeldin A wash-out despite impairment of clathrin function by AP20187. (nih.gov)
  • [ 32 ] Lysis of the endosomes leads to escape and the cytosolic Ad is then transported along the microtubule cytoskeleton, as a result of Ad5 hexon directly binding to dynein intermediate and light chains, and travels towards the perinuclear microtubule organizing centers. (medscape.com)
  • Thus, this Arf6-associated endosomal membrane system parallels and intersects with the clathrin pathway. (nih.gov)
  • HN - 2001 MH - Amino Acids, Neutral UI - D021542 MN - D12.125.154 MS - Amino acids with uncharged R groups or side chains. (nih.gov)
  • With FRET-CLEM, we measure conformational changes in clathrin at thousands of individual morphologically distinct clathrin-coated structures. (nih.gov)
  • In summary, AP promotes clathrin reassembly into coat structures of uniform size and distinctive composition under physiologically relevant salt, temperature, and pH conditions. (rupress.org)
  • The highly conserved clathrin light chain A, whose function has been elusive, promotes integrin-mediated signaling, association of clathrin with the WAVE complex, and efficient cell spreading and migration. (biologists.com)
  • In contrast, coats formed from clathrin alone, under permissive buffer conditions, are larger (400S), more heterogeneous in size (101 nm +/- 15 nm SD), and are composed only of clathrin and its associated light chains. (rupress.org)
  • The structure and spontaneous curvature of clathrin lattices at the plasma membrane. (nih.gov)
  • After internalization, a fraction of this membrane is recycled back to the plasma membrane in an Arf6-dependent manner, and another fraction of this membrane fuses with membrane internalized via the clathrin pathway. (nih.gov)