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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.


supervillin, SVIL, Archvillin
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Actin, gelsolin, CAN, V1a, IIa
Papers on supervillin
Characterization of cells cultured from chylous effusion from a patient with sporadic lymphangioleiomyomatosis.
Dziegiel et al., Kraków, Poland. In Anticancer Res, Jun 2015
A particular pattern of gene expression, including high expression of ezrin (EZR), myosin heavy chain 10, non-muscle (MYH10), and myosin light chain kinase (MYLK) and a greatly decreased expression of supervillin (SVIL), when compared to controls, indicates a high potential motility activity, especially of cell spreading.
Gamma-sarcoglycan is required for the response of archvillin to mechanical stimulation in skeletal muscle.
Barton et al., Worcester, United States. In Hum Mol Genet, Jun 2015
To uncover γ-SG signaling pathway components, we performed yeast two-hybrid screens and identified the muscle-specific protein archvillin as a γ-SG and dystrophin interacting protein.
Molecular toggle switch of histone demethylase LSD1.
Song et al., Baltimore, United States. In Mol Cell, Apr 2015
(2015) demonstrated that a neuron-enriched isoform of LSD1 (LSD1+8a) within a SVIL-containing complex exhibits H3K9me1/2-specific demethylation activity.
A specific LSD1/KDM1A isoform regulates neuronal differentiation through H3K9 demethylation.
Shi et al., Boston, United States. In Mol Cell, Apr 2015
Instead, LSD1+8a mediates H3K9me2 demethylation in collaboration with supervillin (SVIL), a new LSD1+8a interacting protein.
Supervillin binds the Rac/Rho-GEF Trio and increases Trio-mediated Rac1 activation.
Luna et al., Worcester, United States. In Cytoskeleton (hoboken), 2015
We investigated cross-talk between the membrane-associated, myosin II-regulatory protein supervillin and the actin-regulatory small GTPases Rac1, RhoA, and Cdc42.
Analysis of genes involved in response to doxorubicin and a GD2 ganglioside-specific 14G2a monoclonal antibody in IMR-32 human neuroblastoma cells.
Rokita et al., Kraków, Poland. In Acta Biochim Pol, 2014
Next, we used RT-PCR to verify mRNA levels of selected DOX-responsive genes such as RPS27L, PPM1D, SESN1, CDKN1A, TNFSF10B, and 14G2a-responsive genes such as SVIL, JUN, RASSF6, TLX2, ID1.
Sphingosine kinase 1 isoform-specific interactions in breast cancer.
McGowan et al., Sydney, Australia. In Mol Endocrinol, 2014
Many of the novel identified SK1 interaction partners such as supervillin, drebrin, and the myristoylated alanine-rich C-kinase substrate-related protein supported and highlighted previously implicated roles of SK1 in breast cancer cell migration, adhesion, and cytoskeletal remodeling.
Supervillin binding to myosin II and synergism with anillin are required for cytokinesis.
Luna et al., Shrewsbury, United States. In Mol Biol Cell, 2013
Most known regulators act during late cytokinesis; a few, including the myosin II-binding proteins anillin and supervillin, act earlier.
The expanding superfamily of gelsolin homology domain proteins.
Robinson et al., Singapore, Singapore. In Cytoskeleton (hoboken), 2013
In humans, three copies of the domain are present in CapG, five copies in supervillin, and six copies each in adseverin, gelsolin, flightless I and the villins: villin, advillin and villin-like protein.
The role of PLK1-phosphorylated SVIL in myosin II activation and cytokinetic furrowing.
Senga et al., Nagoya, Japan. In J Cell Sci, 2013
In this report, we show that an actin/myosin-II-binding protein, supervillin (SVIL), is a substrate of PLK1.
Gelsolin: the tail of a molecular gymnast.
Burtnick et al., Singapore, Singapore. In Cytoskeleton (hoboken), 2013
Supervillin, which lacks the severing domain 1 and the F-actin binding-site on domain 2, is the clear exception.
Human genome-wide association and mouse knockout approaches identify platelet supervillin as an inhibitor of thrombus formation under shear stress.
Bray et al., Philadelphia, United States. In Circulation, 2012
Human genome-wide association and mouse knockout approaches identify platelet supervillin as an inhibitor of thrombus formation under shear stress.
Association of supervillin with KIR2DL1 regulates the inhibitory signaling of natural killer cells.
Ge et al., Shanghai, China. In Cell Signal, 2011
supervillin is a novel molecule that associates with KIR2DL1 receptor and regulates the inhibitory signaling in NK cells.
Novel interactors and a role for supervillin in early cytokinesis.
Luna et al., Worcester, United States. In Cytoskeleton (hoboken), 2010
Supervillin, like its interactors, is important for efficient cytokinesis.
The membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility.
Luna et al., Worcester, United States. In Traffic, 2010
supervillin, F-actin and associated proteins coordinate a rapid, basolateral membrane recycling pathway that contributes to ERK signaling and actin-based cell motility
How to arm a supervillin: designing F-actin binding activity into supervillin headpiece.
McKnight et al., Boston, United States. In J Mol Biol, 2009
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.
Regulation of cell structure and function by actin-binding proteins: villin's perspective.
George et al., Memphis, United States. In Febs Lett, 2008
It belongs to a large family of actin-binding proteins which includes actin-capping, -nucleating and/or -severing proteins such as gelsolin, severin, fragmin, adseverin/scinderin and actin crosslinking proteins such as dematin and supervillin.
Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators.
Campbell et al., Canberra, Australia. In Bioessays, 2005
In particular, flightless I, supervillin and gelsolin itself have roles as coactivators for nuclear receptors, despite the fact that their divergence appears to predate the evolutionary appearance of nuclear receptors.
The flightless I protein and the gelsolin family in nuclear hormone receptor-mediated signalling.
Campbell et al., Canberra, Australia. In Biochem Soc Trans, 2004
Recent studies indicate that supervillin, gelsolin and FliI are involved in intracellular signalling via nuclear hormone receptors including the androgen, oestrogen and thyroid hormone receptors.
Gelsolin superfamily proteins: key regulators of cellular functions.
Hayoz et al., Lausanne, Switzerland. In Cell Mol Life Sci, 2004
Gelsolin is the founding member of this family, which now contains at least another six members: villin, adseverin, capG, advillin, supervillin and flightless I.
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