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SVIL encodes a bipartite protein with distinct amino- and carboxy-terminal domains. Additionally we are shipping Supervillin Antibodies (41) and Supervillin Proteins (5) and many more products for this protein.
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SVIL regulates neuronal maturation by controlling LSD1+8a mediated histone H3K9 demethylation.
These results position archvillin as a mechanically sensitive component of the dystrophin complex and demonstrate that signaling defects caused by loss of gamma-SG occur both at the sarcolemma and in the nucleus.
Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin additively increases cell division failure.
An actin/myosin-II-binding protein, supervillin (SVIL), is a substrate of PLK1.
adhesion regulatory protein supervillin increases cell survival by decreasing levels of the tumor suppressor protein p53 and downstream target genes
Human genome-wide association and mouse knockout approaches identify platelet supervillin as an inhibitor of thrombus formation under shear stress.
supervillin is a novel molecule that associates with KIR2DL1 receptor and regulates the inhibitory signaling in NK cells.
Supervillin, like its interactors, is important for efficient cytokinesis.
supervillin, F-actin and associated proteins coordinate a rapid, basolateral membrane recycling pathway that contributes to ERK signaling and actin-based cell motility
Supervillin associates with androgen receptor and modulates its transcriptional activity.
archvillin is among the first costameric proteins to assemble during myogenesis and that it contributes to myogenic membrane structure and differentiation.
These data suggest a model in which archvillin attaches directly to the Z-line of skeletal muscle through an interaction with the nebulin C-terminus.
SV is a component of podosomes and invadopodia and SV plays a role in invadopodial function, perhaps as a mediator of cortactin localization, activation state, and/or dynamics of metalloproteinases at the ventral cell surface.
The first NMR solution structure and (15)N-relaxation analysis of a villin-type headpiece domain natively devoid of F-actin binding activity, that of supervillin headpiece (SVHP), is shown.
supervillin (SV)--a peripheral membrane protein that binds myosin II and F-actin in such cells--negatively regulates stress fibers, focal adhesions, and cell-substrate adhesion
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. 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. The encoded protein appears to aid in both myosin II assembly during cell spreading and disassembly of focal adhesions. Two transcript variants encoding different isoforms of supervillin have been described.
, membrane-associated F-actin binding protein p205
, supervillin muscle-specific isoform