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| Aliases | SVIL , supervillin, MFM10 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 604126 MGI: 2147319 HomoloGene: 25090 GeneCards: SVIL | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Supervillin is a protein that in humans is encoded by the SVIL gene. [5] [6]
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| Aliases | SVIL , supervillin, MFM10 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 604126 MGI: 2147319 HomoloGene: 25090 GeneCards: SVIL | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Supervillin is a protein that in humans is encoded by the SVIL gene. [5] [6]
This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments. [7] The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. Its function may include recruitment of actin and other cytoskeletal proteins into specialized structures at the plasma membrane and in the nuclei of growing cells. Two transcript variants encoding different isoforms of supervillin have been described. [6]
SVIL has been shown to interact with Androgen receptor. [8]
The androgen receptor (AR), also known as NR3C4, is a type of nuclear receptor that is activated by binding any of the androgenic hormones, including testosterone and dihydrotestosterone, in the cytoplasm and then translocating into the nucleus. The androgen receptor is most closely related to the progesterone receptor, and progestins in higher dosages can block the androgen receptor.
In mammalian cells, vinculin is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane.
Gelsolin is an actin-binding protein that is a key regulator of actin filament assembly and disassembly. Gelsolin is one of the most potent members of the actin-severing gelsolin/villin superfamily, as it severs with nearly 100% efficiency.
Cortactin is a monomeric protein located in the cytoplasm of cells that can be activated by external stimuli to promote polymerization and rearrangement of the actin cytoskeleton, especially the actin cortex around the cellular periphery. It is present in all cell types. When activated, it will recruit Arp2/3 complex proteins to existing actin microfilaments, facilitating and stabilizing nucleation sites for actin branching. Cortactin is important in promoting lamellipodia formation, invadopodia formation, cell migration, and endocytosis.
Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.
Transforming growth factor beta-1-induced transcript 1 protein is a protein that in humans is encoded by the TGFB1I1 gene. Often put together with and studied alongside TGFB1I1 is the mouse homologue HIC-5. As the name suggests, TGFB1I1 is an induced form of the larger family of TGFB1. Studies suggest TGFB1I1 plays a role in processes of cell growth, proliferation, migration, differentiation and senescence. TGFB1I1 is most localized at focal adhesion complexes of cells, although it may be found active in the cytosol, nucleus and cell membrane as well.
Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene.
Dynamin-2 is a protein that in humans is encoded by the DNM2 gene.
Syntaxin-4 is a protein that in humans is encoded by the STX4 gene.
Actin, cytoplasmic 2, or gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity.
Probable G-protein coupled receptor 158 (GPR158), also known as the metabotropic glycine receptor (mGlyR), is a protein that in humans is encoded by the GPR158 gene.
Moesin is a protein that in humans is encoded by the MSN gene.
Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene.
Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.
Spectrin beta chain, brain 1 is a protein that in humans is encoded by the SPTBN1 gene.
CD2-associated protein is a protein that in humans is encoded by the CD2AP gene.
Formin-binding protein 1 is a protein that in humans is encoded by the FNBP1 gene.
Scinderin is a protein that in humans is encoded by the SCIN gene. Scinderin is an actin severing protein belonging to the gelsolin superfamily. It was discovered in Dr. Trifaro's laboratory at the University of Ottawa, Canada. Secretory tissues are rich in scinderin. In these tissues scinderin, a calcium dependent protein, regulates cortical actin networks. Normally secretory vesicles are excluded from release sites on the plasma membrane by the presence of a cortical actin filament network. During cell stimulation, calcium channels open allowing calcium ions to enter the secretory cell. Increase in intracellular calcium activates scinderin with the consequent actin filament severing and local dissociation of actin filament networks. This allows the movement of secretory vesicles to release sites on the plasma membrane.
Guanine nucleotide-binding protein subunit alpha-13 is a protein that in humans is encoded by the GNA13 gene.
In molecular biology, the FERM domain is a widespread protein module involved in localising proteins to the plasma membrane. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus in the majority of proteins in which it is found.
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