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    SVIL supervillin [ Homo sapiens (human) ]

    Gene ID: 6840, updated on 7-Jul-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Supervillin Contributes to LPS-induced Inflammatory Response in THP-1 Cell-derived Macrophages.

    Supervillin Contributes to LPS-induced Inflammatory Response in THP-1 Cell-derived Macrophages.
    Zhou J, Que Y, Pan L, Li X, Zhu C, Jin L, Li S.

    03/26/2022
    Molecular basis of functional exchangeability between ezrin and other actin-membrane associated proteins during cytokinesis.

    Molecular basis of functional exchangeability between ezrin and other actin-membrane associated proteins during cytokinesis.
    Yang G, Hiruma S, Kitamura A, Kinjo M, Mishra M, Uehara R.

    09/25/2021
    A twinpair analysis indicates congenital scoliosis is associated with allelespecific methylation in the SVIL gene.

    A twin‑pair analysis indicates congenital scoliosis is associated with allele‑specific methylation in the SVIL gene.
    Zhang Z, Chen Y, Wu Y, Hao Y, Zhao X, Wang X, Wang Y, Xi Y, Zhang X.

    04/24/2021
    Supervillin promotes tumor angiogenesis in liver cancer.

    Supervillin promotes tumor angiogenesis in liver cancer.
    Zhao C, Zhao Z, Wang Z, Hu L, Wang H, Fang Z., Free PMC Article

    03/13/2021
    Loss of supervillin causes myopathy with myofibrillar disorganization and autophagic vacuoles.

    Loss of supervillin causes myopathy with myofibrillar disorganization and autophagic vacuoles.
    Hedberg-Oldfors C, Meyer R, Nolte K, Abdul Rahim Y, Lindberg C, Karason K, Thuestad IJ, Visuttijai K, Geijer M, Begemann M, Kraft F, Lausberg E, Hitpass L, Götzl R, Luna EJ, Lochmüller H, Koschmieder S, Gramlich M, Gess B, Elbracht M, Weis J, Kurth I, Oldfors A, Knopp C., Free PMC Article

    01/2/2021
    SVIL regulates neuronal maturation by controlling LSD1+8a mediated histone H3K9 demethylation.

    A specific LSD1/KDM1A isoform regulates neuronal differentiation through H3K9 demethylation.
    Laurent B, Ruitu L, Murn J, Hempel K, Ferrao R, Xiang Y, Liu S, Garcia BA, Wu H, Wu F, Steen H, Shi Y., Free PMC Article

    04/30/2016
    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.

    Gamma-sarcoglycan is required for the response of archvillin to mechanical stimulation in skeletal muscle.
    Spinazzola JM, Smith TC, Liu M, Luna EJ, Barton ER., Free PMC Article

    12/26/2015
    Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin additively increases cell division failure.

    Supervillin binding to myosin II and synergism with anillin are required for cytokinesis.
    Smith TC, Fridy PC, Li Y, Basil S, Arjun S, Friesen RM, Leszyk J, Chait BT, Rout MP, Luna EJ., Free PMC Article

    06/28/2014
    An actin/myosin-II-binding protein, supervillin (SVIL), is a substrate of PLK1.

    The role of PLK1-phosphorylated SVIL in myosin II activation and cytokinetic furrowing.
    Hasegawa H, Hyodo T, Asano E, Ito S, Maeda M, Kuribayashi H, Natsume A, Wakabayashi T, Hamaguchi M, Senga T.

    06/21/2014
    adhesion regulatory protein supervillin increases cell survival by decreasing levels of the tumor suppressor protein p53 and downstream target genes

    Supervillin-mediated suppression of p53 protein enhances cell survival.
    Fang Z, Luna EJ., Free PMC Article

    05/18/2013
    Human genome-wide association and mouse knockout approaches identify platelet supervillin as an inhibitor of thrombus formation under shear stress.

    Human genome-wide association and mouse knockout approaches identify platelet supervillin as an inhibitor of thrombus formation under shear stress.
    Edelstein LC, Luna EJ, Gibson IB, Bray M, Jin Y, Kondkar A, Nagalla S, Hadjout-Rabi N, Smith TC, Covarrubias D, Jones SN, Ahmad F, Stolla M, Kong X, Fang Z, Bergmeier W, Shaw C, Leal SM, Bray PF., Free PMC Article

    09/15/2012
    supervillin is a novel molecule that associates with KIR2DL1 receptor and regulates the inhibitory signaling in NK cells.

    Association of supervillin with KIR2DL1 regulates the inhibitory signaling of natural killer cells.
    Liu HP, Yu MC, Jiang MH, Chen JX, Yan DP, Liu F, Ge BX.

    04/16/2011
    Supervillin, like its interactors, is important for efficient cytokinesis.

    Novel interactors and a role for supervillin in early cytokinesis.
    Smith TC, Fang Z, Luna EJ., Free PMC Article

    10/4/2010
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
    supervillin, F-actin and associated proteins coordinate a rapid, basolateral membrane recycling pathway that contributes to ERK signaling and actin-based cell motility

    The membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility.
    Fang Z, Takizawa N, Wilson KA, Smith TC, Delprato A, Davidson MW, Lambright DG, Luna EJ., Free PMC Article

    06/28/2010
    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.

    How to arm a supervillin: designing F-actin binding activity into supervillin headpiece.
    Brown JW, Vardar-Ulu D, McKnight CJ., Free PMC Article

    01/21/2010
    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.

    Supervillin reorganizes the actin cytoskeleton and increases invadopodial efficiency.
    Crowley JL, Smith TC, Fang Z, Takizawa N, Luna EJ., Free PMC Article

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (3) articles

    Single nucleotide polymorphisms of microRNA machinery genes modify the risk of renal cell carcinoma.
    Horikawa Y, Wood CG, Yang H, Zhao H, Ye Y, Gu J, Lin J, Habuchi T, Wu X.

    KIF5B gene sequence variation and response of cardiac stroke volume to regular exercise.
    Argyropoulos G, Stütz AM, Ilnytska O, Rice T, Teran-Garcia M, Rao DC, Bouchard C, Rankinen T.

    A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease.
    Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs AL, Smemo S, Kauwe JS, Maxwell TJ, Cherny S, Doil L, Tacey K, van Luchene R, Myers A, Wavrant-De Vrièze F, Kaleem M, Hollingworth P, Jehu L, Foy C, Archer N, Hamilton G, Holmans P, Morris CM, Catanese J, Sninsky J, White TJ, Powell J, Hardy J, O'Donovan M, Lovestone S, Jones L, Morris JC, Thal L, Owen M, Williams J, Goate A.

    01/11/2009
    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.

    Archvillin anchors in the Z-line of skeletal muscle via the nebulin C-terminus.
    Lee MA, Joo YM, Lee YM, Kim HS, Kim JH, Choi JK, Ahn SJ, Min BI, Kim CR.

    01/21/2010
    Supervillin associates with androgen receptor and modulates its transcriptional activity.

    Supervillin associates with androgen receptor and modulates its transcriptional activity.
    Ting HJ, Yeh S, Nishimura K, Chang C., Free PMC Article

    01/21/2010
    archvillin is among the first costameric proteins to assemble during myogenesis and that it contributes to myogenic membrane structure and differentiation.

    Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton.
    Oh SW, Pope RK, Smith KP, Crowley JL, Nebl T, Lawrence JB, Luna EJ.

    01/21/2010
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