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    Fermt2 fermitin family member 2 [ Mus musculus (house mouse) ]

    Gene ID: 218952, updated on 6-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    In a mouse model of wound healing, KINDLIN-2 gene knockdown inhibited wound healing, and increased neovascular permeability in vivo.

    Knockdown of the KINDLIN-2 Gene and Reduced Expression of Kindlin-2 Affects Vascular Permeability in Angiogenesis in a Mouse Model of Wound Healing.
    Ying J, Luan W, Lu L, Zhang S, Qi F., Free PMC Article

    11/10/2018
    Our studies identify Kindlin-2 as a stabilizing linker of endothelial AJs with the actin cytoskeleton, thereby re-enforcing the vascular barrier.

    Kindlin-2 interacts with endothelial adherens junctions to support vascular barrier integrity.
    Pluskota E, Bledzka KM, Bialkowska K, Szpak D, Soloviev DA, Jones SV, Verbovetskiy D, Plow EF., Free PMC Article

    06/9/2018
    Kindlin-2 is a key protein that couples cell adhesion by activating integrins and the induction of membrane protrusions by activating Rac1 and supplying Rac1 with the Arp2/3 complex.

    Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading.
    Böttcher RT, Veelders M, Rombaut P, Faix J, Theodosiou M, Stradal TE, Rottner K, Zent R, Herzog F, Fässler R., Free PMC Article

    11/25/2017
    demonstration that Smurf1 acts as a brake for integrin activation by controlling Kindlin-2 protein levels, a new mechanism that permits precise modulation of integrin-mediated cellular functions

    Smurf1 inhibits integrin activation by controlling Kindlin-2 ubiquitination and degradation.
    Wei X, Wang X, Zhan J, Chen Y, Fang W, Zhang L, Zhang H., Free PMC Article

    10/7/2017
    Postnatal loss of Kindlin-2 from cardiac myocytes leads to progressive heart failure.

    Postnatal Loss of Kindlin-2 Leads to Progressive Heart Failure.
    Zhang Z, Mu Y, Veevers J, Peter AK, Manso AM, Bradford WH, Dalton ND, Peterson KL, Knowlton KU, Ross RS, Zhou X, Chen J., Free PMC Article

    07/8/2017
    Data indicate that Kindlin-2 not only maintains the cardiac structure but also is required for cardiac function.

    Depletion of Kindlin-2 induces cardiac dysfunction in mice.
    Qi L, Yu Y, Chi X, Lu D, Song Y, Zhang Y, Zhang H.

    07/1/2017
    These findings show that talin and kindlin cooperatively activate integrins leading to fibronectin binding and adhesion.

    Kindlin-2 cooperates with talin to activate integrins and induces cell spreading by directly binding paxillin.
    Theodosiou M, Widmaier M, Böttcher RT, Rognoni E, Veelders M, Bharadwaj M, Lambacher A, Austen K, Müller DJ, Zent R, Fässler R., Free PMC Article

    10/22/2016
    These studies uncover a previously unrecognized function for Kindlin-2 and a mechanism for regulation of the chondrocyte differentiation programme and chondrogenesis.

    Kindlin-2 controls TGF-β signalling and Sox9 expression to regulate chondrogenesis.
    Wu C, Jiao H, Lai Y, Zheng W, Chen K, Qu H, Deng W, Song P, Zhu K, Cao H, Galson DL, Fan J, Im HJ, Liu Y, Chen J, Chen D, Xiao G., Free PMC Article

    04/23/2016
    Taken together, our study suggests the suppressive roles of Kindlin-2 in the pathogenesis of colorectal carcinoma

    Kindlin-2 inhibited the growth and migration of colorectal cancer cells.
    Ren Y, Jin H, Xue Z, Xu Q, Wang S, Zhao G, Huang J, Huang H.

    10/24/2015
    Data suggest that kindlin-2 (Kind2/Fermt2) interacts with actin alpha 2 (Actn2) and integrin beta 1 (Itgb1) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 leads to dissociation of Actn2 and Itgb1.

    Kindlin-2 interacts with α-actinin-2 and β1 integrin to maintain the integrity of the Z-disc in cardiac muscles.
    Qi L, Yu Y, Chi X, Xu W, Lu D, Song Y, Zhang Y, Zhang H.

    10/17/2015
    beta3/kindlin-2 interaction promotes outside-in alphaVbeta3 signaling selectively, with biological consequences in vivo [kindlin-2]

    Interaction of kindlin-2 with integrin β3 promotes outside-in signaling responses by the αVβ3 vitronectin receptor.
    Liao Z, Kato H, Pandey M, Cantor JM, Ablooglu AJ, Ginsberg MH, Shattil SJ., Free PMC Article

    06/18/2015
    kindlin-2 tyrosine phosphorylation and interaction with Src serve as a regulatable switch downstream of focal adhesion kinase in the integrin outside-in signaling circuit controlling cell migration and proliferation

    Kindlin-2 tyrosine phosphorylation and interaction with Src serve as a regulatable switch in the integrin outside-in signaling circuit.
    Qu H, Tu Y, Guan JL, Xiao G, Wu C., Free PMC Article

    01/24/2015
    kindlin-2, through activating Ras and the downstream ERK1/2 and Akt signaling pathways, plays an important role in regulating renal tubular epithelial-to-mesenchymal transition

    Kindlin-2 regulates renal tubular cell plasticity by activation of Ras and its downstream signaling.
    Wei X, Wang X, Xia Y, Tang Y, Li F, Fang W, Zhang H.

    03/8/2014
    C-terminal LIM domains of migfilin dictate its focal adhesion localization, and these domains mediate an interaction with kindlin in vitro and in cells, demonstrating that kindlin is important for normal migfilin dynamics.

    Kindlin binds migfilin tandem LIM domains and regulates migfilin focal adhesion localization and recruitment dynamics.
    Brahme NN, Harburger DS, Kemp-O'Brien K, Stewart R, Raghavan S, Parsons M, Calderwood DA., Free PMC Article

    02/15/2014
    kindlin-2 regulates trafficking of endothelial cell surface enzymes that control platelet responses and hemostasis.

    Kindlin-2 regulates hemostasis by controlling endothelial cell-surface expression of ADP/AMP catabolic enzymes via a clathrin-dependent mechanism.
    Pluskota E, Ma Y, Bledzka KM, Bialkowska K, Soloviev DA, Szpak D, Podrez EA, Fox PL, Hazen SL, Dowling JJ, Ma YQ, Plow EF., Free PMC Article

    11/23/2013
    Kindlin-2 mediates activation of TGF-beta/Smad signaling and renal fibrosis.

    Kindlin-2 mediates activation of TGF-β/Smad signaling and renal fibrosis.
    Wei X, Xia Y, Li F, Tang Y, Nie J, Liu Y, Zhou Z, Zhang H, Hou FF., Free PMC Article

    11/2/2013
    Kindlin has a role in regulating integrin alpha5beta1 surface expression.

    Distinct roles of talin and kindlin in regulating integrin α5β1 function and trafficking.
    Margadant C, Kreft M, de Groot DJ, Norman JC, Sonnenberg A.

    02/23/2013
    Mediation of Rac1 activation by kindlin-2: an essential function in osteoblast adhesion, spreading, and proliferation

    Mediation of Rac1 activation by kindlin-2: an essential function in osteoblast adhesion, spreading, and proliferation.
    Jung GY, Park YJ, Han JS.

    12/10/2011
    Endothelial cells derived from kindlin-2(+/-) mice had integrin expression levels similar to WT mice but reduced alphaVbeta3-dependent signaling, migration, adhesion, spreading, and tube formation.

    The integrin coactivator kindlin-2 plays a critical role in angiogenesis in mice and zebrafish.
    Pluskota E, Dowling JJ, Gordon N, Golden JA, Szpak D, West XZ, Nestor C, Ma YQ, Bialkowska K, Byzova T, Plow EF., Free PMC Article

    07/9/2011
    physiological role for kindlin-2 in skin fibroblasts under normal steady-state conditions and during tissue regeneration

    Role of kindlin-2 in fibroblast functions: implications for wound healing.
    He Y, Esser P, Schacht V, Bruckner-Tuderman L, Has C.

    01/29/2011
    The genomic organization, gene expression and subcellular localization of murine Kindlins-1 to -3, is described.

    The Kindlins: subcellular localization and expression during murine development.
    Ussar S, Wang HV, Linder S, Fässler R, Moser M.

    01/21/2010
    kindlin-2 is a novel integrin adaptor protein important for muscle differentiation, and is a critical regulator of myocyte elongation.

    Kindlin-2 is required for myocyte elongation and is essential for myogenesis.
    Dowling JJ, Vreede AP, Kim S, Golden J, Feldman EL., Free PMC Article

    01/21/2010
    Kindlin-2 is a novel and essential element of bidirectional integrin signaling.

    Kindlin-2 controls bidirectional signaling of integrins.
    Montanez E, Ussar S, Schifferer M, Bösl M, Zent R, Moser M, Fässler R., Free PMC Article

    01/21/2010
    kindlin-2 is an essential component of the intercalated disc, is necessary for cytoskeletal organization at sites of membrane attachment, and is required for vertebrate myocardial formation and function

    Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function.
    Dowling JJ, Gibbs E, Russell M, Goldman D, Minarcik J, Golden JA, Feldman EL.

    01/21/2010
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