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    FERMT3 FERM domain containing kindlin 3 [ Homo sapiens (human) ]

    Gene ID: 83706, updated on 3-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Kindlin-3/FERMT3 is upregulated in atherosclerotic, mainly in cells of monocytic origin and of M2 type. Simultaneous upregulation of ITGB2 suggests a synergistic effect on leukocyte adherence and transmigration into the vessel wall.

    Kindlin 3 (FERMT3) is associated with unstable atherosclerotic plaques, anti-inflammatory type II macrophages and upregulation of beta-2 integrins in all major arterial beds.
    Oksala N, Pärssinen J, Seppälä I, Klopp N, Illig T, Laaksonen R, Levula M, Raitoharju E, Kholova I, Sioris T, Kähönen M, Lehtimäki T, Hytönen VP.

    05/28/2016
    The accumulation of HSPCs in the circulation of leukocyte adhesion deficiency type III patients, who lack Kindlin-3, underlines the conserved functions of Kindlin-3 in man and the importance of our findings for human disease.

    Kindlin-3-mediated integrin adhesion is dispensable for quiescent but essential for activated hematopoietic stem cells.
    Ruppert R, Moser M, Sperandio M, Rognoni E, Orban M, Liu WH, Schulz AS, Oostendorp RA, Massberg S, Fässler R., Free PMC Article

    11/7/2015
    A new C>T point mutation was found in exon 13 in the FERMT3 gene in an infant diagnosed with LAD-III. KINDLIN-3 expression is required for platelet aggregation and leukocyte function, but also osteoclast-mediated bone resorption.

    A new mutation in the KINDLIN-3 gene ablates integrin-dependent leukocyte, platelet, and osteoclast function in a patient with leukocyte adhesion deficiency-III.
    Crazzolara R, Maurer K, Schulze H, Zieger B, Zustin J, Schulz AS.

    10/17/2015
    Mig-2 significantly attenuates the antitumor action of cisplatin.

    Mig-2 attenuates cisplatin-induced apoptosis of human glioma cells in vitro through AKT/JNK and AKT/p38 signaling pathways.
    Ou YW, Zhao ZT, Wu CY, Xu BN, Song YM, Zhan QM., Free PMC Article

    09/5/2015
    The data uncover a novel and unexpected tumor suppressor role of Kindlin-3 which can influence integrins targeted therapies development.

    A novel tumor suppressor function of Kindlin-3 in solid cancer.
    Djaafri I, Khayati F, Menashi S, Tost J, Podgorniak MP, Sadoux A, Daunay A, Teixeira L, Soulier J, Idbaih A, Setterblad N, Fauvel F, Calvo F, Janin A, Lebbé C, Mourah S., Free PMC Article

    08/8/2015
    High Kindlin-2 expression promotes pancreatic ductal adenocarcinoma progression.

    Kindlin-2 induced by TGF-β signaling promotes pancreatic ductal adenocarcinoma progression through downregulation of transcriptional factor HOXB9.
    Zhan J, Song J, Wang P, Chi X, Wang Y, Guo Y, Fang W, Zhang H.

    05/23/2015
    These data identify a role of kindlin-3 phosphorylation in integrin b3 activation and provide a basis for functional differences between kindlin-3 and the two other kindlin paralogs.

    Site-specific phosphorylation of kindlin-3 protein regulates its capacity to control cellular responses mediated by integrin αIIbβ3.
    Bialkowska K, Byzova TV, Plow EF., Free PMC Article

    05/23/2015
    Kindlin 2 expression was significantly increased in luteinized granulosa cells from patients with polycystic ovary syndrome.

    Increased expression of kindlin 2 in luteinized granulosa cells correlates with androgen receptor level in patients with polycystic ovary syndrome having hyperandrogenemia.
    Yang M, Du J, Lu D, Ren C, Shen H, Qiao J, Chen X, Zhang H., Free PMC Article

    04/18/2015
    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
    Direct activation of RhoA with recombinant bacterial cytotoxic necrotizing factor y reverted the abnormal phenotype and barrier function of kindlin-2-deficient keratinocytes and skin equivalents.

    RhoA activation by CNFy restores cell-cell adhesion in kindlin-2-deficient keratinocytes.
    He Y, Sonnenwald T, Sprenger A, Hansen U, Dengjel J, Bruckner-Tuderman L, Schmidt G, Has C.

    08/9/2014
    ADAP interacts with talin and kindlin-3 to promote platelet Integrin alphaIIbbeta3 activation and stable fibrinogen binding.

    ADAP interactions with talin and kindlin promote platelet integrin αIIbβ3 activation and stable fibrinogen binding.
    Kasirer-Friede A, Kang J, Kahner B, Ye F, Ginsberg MH, Shattil SJ., Free PMC Article

    07/19/2014
    Kindlin-3 influences breast cancer progression by influencing the crosstalk between beta1 integrins and Twist to increase VEGF production, which enhances breast cancer cell invasion and tumor angiogenesis and metastasis

    Kindlin-3 enhances breast cancer progression and metastasis by activating Twist-mediated angiogenesis.
    Sossey-Alaoui K, Pluskota E, Davuluri G, Bialkowska K, Das M, Szpak D, Lindner DJ, Downs-Kelly E, Thompson CL, Plow EF., Free PMC Article

    06/21/2014
    While Kindlin-2 was highly expressed in control tissues, a drastic low expression of Kindlin-2 was found in the tumor tissues of serous epithelial ovarian cancer, especially in high-grade serous epithelial ovarian cancer.

    Kindlin-2 inhibits serous epithelial ovarian cancer peritoneal dissemination and predicts patient outcomes.
    Ren C, Du J, Xi C, Yu Y, Hu A, Zhan J, Guo H, Fang W, Liu C, Zhang H.

    06/14/2014
    kindlin-3-mediated high-affinity LFA-1 controls both the early transient integrin-dependent adhesions in addition to the final stable adhesions made under flow conditions

    Novel automated tracking analysis of particles subjected to shear flow: kindlin-3 role in B cells.
    Willenbrock F, Zicha D, Hoppe A, Hogg N., Free PMC Article

    04/19/2014
    the beta-2-integrin-kindlin-3 interaction is particularly important in adhesion strengthening under shear flow, and for T-cell homing to lymph nodes, but dispensable for T cell activation which occurs in a shear-free environment

    The β2 integrin-kindlin-3 interaction is essential for T-cell homing but dispensable for T-cell activation in vivo.
    Morrison VL, MacPherson M, Savinko T, Lek HS, Prescott A, Fagerholm SC., Free PMC Article

    11/16/2013
    kindlin-3 is required for the integrin alphaMbeta2-Syk-Vav1 signaling axis that regulates Rac1 and Cdc42 activities. These findings reinforce a role for kindlin-3 in integrin outside-in signaling.

    A role of kindlin-3 in integrin αMβ2 outside-in signaling and the Syk-Vav1-Rac1/Cdc42 signaling axis.
    Xue ZH, Feng C, Liu WL, Tan SM., Free PMC Article

    08/31/2013
    the correct functioning of the kindlin 3 PH domain is central to the role that kindlin 3 performs in guiding lymphocyte adhesion and motility behavior, which in turn is required for a successful immune response.

    The kindlin 3 pleckstrin homology domain has an essential role in lymphocyte function-associated antigen 1 (LFA-1) integrin-mediated B cell adhesion and migration.
    Hart R, Stanley P, Chakravarty P, Hogg N., Free PMC Article

    08/10/2013
    Agonist stimulation, talin-1, and kindlin-3 are crucial for alpha(IIb)beta(3) activation in a human megakaryoblastic cell line, CMK.

    Agonist stimulation, talin-1, and kindlin-3 are crucial for α(IIb)β(3) activation in a human megakaryoblastic cell line, CMK.
    Nakazawa T, Tadokoro S, Kamae T, Kiyomizu K, Kashiwagi H, Honda S, Kanakura Y, Tomiyama Y.

    03/30/2013
    cleavage of Kindlin-3 by calpain controls the dynamics of integrin-Kindlin-3 interaction and as a result, integrin-dependent adhesion and migration of hematopoietic cells.

    Regulation of cell adhesion and migration by Kindlin-3 cleavage by calpain.
    Zhao Y, Malinin NL, Meller J, Ma Y, West XZ, Bledzka K, Qin J, Podrez EA, Byzova TV., Free PMC Article

    02/23/2013
    Multivalent LFA-1/ICAM-1 bonds serve as mechanosensors that direct PMN cytoskeletal activity by transmission of tensile force to a supramolecular complex that triggers Ca2+ influx at sites of adhesive contact.

    Leukocyte function antigen-1, kindlin-3, and calcium flux orchestrate neutrophil recruitment during inflammation.
    Dixit N, Kim MH, Rossaint J, Yamayoshi I, Zarbock A, Simon SI., Free PMC Article

    02/23/2013
    kindlin-3 lowers the threshold for NK cell activation. Loss of kindlin-3 has a pronounced effect on NK cell-mediated cytotoxicity triggered by single activating receptors.

    Loss of kindlin-3 alters the threshold for NK cell activation in human leukocyte adhesion deficiency-III.
    Gruda R, Brown AC, Grabovsky V, Mizrahi S, Gur C, Feigelson SW, Achdout H, Bar-On Y, Alon R, Aker M, Davis DM, Mandelboim O.

    01/26/2013
    Kindlin-3 deficiency impairs integrin function, including activation of beta(1) integrin. Abnormalities in glycoprotein Ib-IX function in Kindlin-3-deficient platelets are secondary to integrin defects

    Novel aspects of Kindlin-3 function in humans based on a new case of leukocyte adhesion deficiency III.
    Meller J, Malinin NL, Panigrahi S, Kerr BA, Patil A, Ma Y, Venkateswaran L, Rogozin IB, Mohandas N, Ehlayel MS, Podrez EA, Chinen J, Byzova TV., Free PMC Article

    12/29/2012
    integrin alphaLbeta2 engagement by its ligand ICAM-1 promotes the association of kindlin-3 with RACK1

    Kindlin-3 mediates integrin αLβ2 outside-in signaling, and it interacts with scaffold protein receptor for activated-C kinase 1 (RACK1).
    Feng C, Li YF, Yau YH, Lee HS, Tang XY, Xue ZH, Zhou YC, Lim WM, Cornvik TC, Ruedl C, Shochat SG, Tan SM., Free PMC Article

    09/22/2012
    LAD-III syndrome is caused by mutations in FERMT3, encoding the kindlin-3 protein in all blood cells that is involved in the regulation of beta integrin conformation. (Review)

    Hematologically important mutations: leukocyte adhesion deficiency (first update).
    van de Vijver E, Maddalena A, Sanal Ö, Holland SM, Uzel G, Madkaikar M, de Boer M, van Leeuwen K, Köker MY, Parvaneh N, Fischer A, Law SK, Klein N, Tezcan FI, Unal E, Patiroglu T, Belohradsky BH, Schwartz K, Somech R, Kuijpers TW, Roos D., Free PMC Article

    09/15/2012
    TIIICBP and kindlin-3 could be the same protein and propose a key role for kindlin-3 in platelet activation by type III collagen.

    Platelet type III collagen binding protein (TIIICBP) presents high biochemical and functional similarities with kindlin-3.
    Djaafri I, Maurice P, Labas V, Vinh J, Lemesle M, Arbeille B, Legrand C, Mourah S, Fauvel-Lafeve F.

    06/16/2012