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Journal Abstract Search


385 related items for PubMed ID: 22072711

  • 1. Polarity-regulating kinase partitioning-defective 1b (PAR1b) phosphorylates guanine nucleotide exchange factor H1 (GEF-H1) to regulate RhoA-dependent actin cytoskeletal reorganization.
    Yamahashi Y, Saito Y, Murata-Kamiya N, Hatakeyama M.
    J Biol Chem; 2011 Dec 30; 286(52):44576-84. PubMed ID: 22072711
    [Abstract] [Full Text] [Related]

  • 2. Dynamic regulation of GEF-H1 localization at microtubules by Par1b/MARK2.
    Yoshimura Y, Miki H.
    Biochem Biophys Res Commun; 2011 May 06; 408(2):322-8. PubMed ID: 21513698
    [Abstract] [Full Text] [Related]

  • 3. Guanine nucleotide exchange factor-H1 regulates cell migration via localized activation of RhoA at the leading edge.
    Nalbant P, Chang YC, Birkenfeld J, Chang ZF, Bokoch GM.
    Mol Biol Cell; 2009 Sep 06; 20(18):4070-82. PubMed ID: 19625450
    [Abstract] [Full Text] [Related]

  • 4. Role of guanine nucleotide exchange factor-H1 in complement-mediated RhoA activation in glomerular epithelial cells.
    Mouawad F, Aoudjit L, Jiang R, Szaszi K, Takano T.
    J Biol Chem; 2014 Feb 14; 289(7):4206-18. PubMed ID: 24356971
    [Abstract] [Full Text] [Related]

  • 5. Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton.
    Krendel M, Zenke FT, Bokoch GM.
    Nat Cell Biol; 2002 Apr 14; 4(4):294-301. PubMed ID: 11912491
    [Abstract] [Full Text] [Related]

  • 6. GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases.
    Birkenfeld J, Nalbant P, Bohl BP, Pertz O, Hahn KM, Bokoch GM.
    Dev Cell; 2007 May 14; 12(5):699-712. PubMed ID: 17488622
    [Abstract] [Full Text] [Related]

  • 7. Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules.
    van Horck FP, Ahmadian MR, Haeusler LC, Moolenaar WH, Kranenburg O.
    J Biol Chem; 2001 Feb 16; 276(7):4948-56. PubMed ID: 11058585
    [Abstract] [Full Text] [Related]

  • 8. GEF-H1 couples nocodazole-induced microtubule disassembly to cell contractility via RhoA.
    Chang YC, Nalbant P, Birkenfeld J, Chang ZF, Bokoch GM.
    Mol Biol Cell; 2008 May 16; 19(5):2147-53. PubMed ID: 18287519
    [Abstract] [Full Text] [Related]

  • 9. Spatiotemporal dynamics of GEF-H1 activation controlled by microtubule- and Src-mediated pathways.
    Azoitei ML, Noh J, Marston DJ, Roudot P, Marshall CB, Daugird TA, Lisanza SL, Sandí MJ, Ikura M, Sondek J, Rottapel R, Hahn KM, Danuser G.
    J Cell Biol; 2019 Sep 02; 218(9):3077-3097. PubMed ID: 31420453
    [Abstract] [Full Text] [Related]

  • 10. MARK3-mediated phosphorylation of ARHGEF2 couples microtubules to the actin cytoskeleton to establish cell polarity.
    Sandí MJ, Marshall CB, Balan M, Coyaud É, Zhou M, Monson DM, Ishiyama N, Chandrakumar AA, La Rose J, Couzens AL, Gingras AC, Raught B, Xu W, Ikura M, Morrison DK, Rottapel R.
    Sci Signal; 2017 Oct 31; 10(503):. PubMed ID: 29089450
    [Abstract] [Full Text] [Related]

  • 11. Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA.
    Jiu Y, Peränen J, Schaible N, Cheng F, Eriksson JE, Krishnan R, Lappalainen P.
    J Cell Sci; 2017 Mar 01; 130(5):892-902. PubMed ID: 28096473
    [Abstract] [Full Text] [Related]

  • 12. The RhoA activator GEF-H1/Lfc is a transforming growth factor-beta target gene and effector that regulates alpha-smooth muscle actin expression and cell migration.
    Tsapara A, Luthert P, Greenwood J, Hill CS, Matter K, Balda MS.
    Mol Biol Cell; 2010 Mar 15; 21(6):860-70. PubMed ID: 20089843
    [Abstract] [Full Text] [Related]

  • 13. p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor.
    Zenke FT, Krendel M, DerMardirossian C, King CC, Bohl BP, Bokoch GM.
    J Biol Chem; 2004 Apr 30; 279(18):18392-400. PubMed ID: 14970201
    [Abstract] [Full Text] [Related]

  • 14. HUNK inhibits epithelial-mesenchymal transition of CRC via direct phosphorylation of GEF-H1 and activating RhoA/LIMK-1/CFL-1.
    Han X, Jiang S, Gu Y, Ding L, Zhao E, Cao D, Wang X, Wen Y, Pan Y, Yan X, Duan L, Sun M, Zhou T, Liu Y, Hu H, Ye Q, Gao S.
    Cell Death Dis; 2023 May 16; 14(5):327. PubMed ID: 37193711
    [Abstract] [Full Text] [Related]

  • 15. The RhoA regulators Myo9b and GEF-H1 are targets of cyclic nucleotide-dependent kinases in platelets.
    Comer S, Nagy Z, Bolado A, von Kriegsheim A, Gambaryan S, Walter U, Pagel O, Zahedi RP, Jurk K, Smolenski A.
    J Thromb Haemost; 2020 Nov 16; 18(11):3002-3012. PubMed ID: 32692911
    [Abstract] [Full Text] [Related]

  • 16. Vincristine enhances amoeboid-like motility via GEF-H1/RhoA/ROCK/Myosin light chain signaling in MKN45 cells.
    Eitaki M, Yamamori T, Meike S, Yasui H, Inanami O.
    BMC Cancer; 2012 Oct 12; 12():469. PubMed ID: 23057787
    [Abstract] [Full Text] [Related]

  • 17. Contribution of guanine exchange factor H1 in phorbol ester-induced apoptosis.
    Chang YC, Lee HH, Chen YJ, Bokoch GM, Chang ZF.
    Cell Death Differ; 2006 Dec 12; 13(12):2023-32. PubMed ID: 16601754
    [Abstract] [Full Text] [Related]

  • 18. ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA.
    Fujishiro SH, Tanimura S, Mure S, Kashimoto Y, Watanabe K, Kohno M.
    Biochem Biophys Res Commun; 2008 Mar 28; 368(1):162-7. PubMed ID: 18211802
    [Abstract] [Full Text] [Related]

  • 19. The epidermal growth factor receptor mediates tumor necrosis factor-alpha-induced activation of the ERK/GEF-H1/RhoA pathway in tubular epithelium.
    Kakiashvili E, Dan Q, Vandermeer M, Zhang Y, Waheed F, Pham M, Szászi K.
    J Biol Chem; 2011 Mar 18; 286(11):9268-79. PubMed ID: 21212278
    [Abstract] [Full Text] [Related]

  • 20. The microtubule-associated Rho activating factor GEF-H1 interacts with exocyst complex to regulate vesicle traffic.
    Pathak R, Delorme-Walker VD, Howell MC, Anselmo AN, White MA, Bokoch GM, Dermardirossian C.
    Dev Cell; 2012 Aug 14; 23(2):397-411. PubMed ID: 22898781
    [Abstract] [Full Text] [Related]


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