메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages

Biochemical and functional characterization of the interaction between liprin-α1 and GIT1: Implications for the regulation of cell motility

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR KINASE; G PROTEIN COUPLED RECEPTOR KINASE INTERACTING PROTEIN 1; INTEGRIN; LIPRIN ALPHA1; MUTANT PROTEIN; PAXILLIN; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RHO GUANINE NUCLEOTIDE EXCHANGE FACTORS; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 79958728726     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020757     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • Le Clainche C, Carlier MF, (2008) Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol Rev 88: 489-513.
    • (2008) Physiol Rev , vol.88 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.F.2
  • 2
    • 33646705915 scopus 로고    scopus 로고
    • The multifunctional GIT family of proteins
    • Hoefen RJ, Berk BC, (2006) The multifunctional GIT family of proteins. J Cell Sci 119: 1469-1475.
    • (2006) J Cell Sci , vol.119 , pp. 1469-1475
    • Hoefen, R.J.1    Berk, B.C.2
  • 3
    • 0031610579 scopus 로고    scopus 로고
    • PAK kinases are directly coupled to the PIX family of nucleotide exchange factors
    • Manser E, Loo TH, Koh CG, Zhao ZS, Chen XQ, et al. (1998) PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. Mol Cell 1: 183-192.
    • (1998) Mol Cell , vol.1 , pp. 183-192
    • Manser, E.1    Loo, T.H.2    Koh, C.G.3    Zhao, Z.S.4    Chen, X.Q.5
  • 4
    • 0033843129 scopus 로고    scopus 로고
    • Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly
    • Zhao ZS, Manser E, Loo TH, Lim L, (2000) Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol Cell Biol 20: 6354-6363.
    • (2000) Mol Cell Biol , vol.20 , pp. 6354-6363
    • Zhao, Z.S.1    Manser, E.2    Loo, T.H.3    Lim, L.4
  • 5
    • 59149097659 scopus 로고    scopus 로고
    • Structures of dimeric GIT1 and trimeric beta-PIX and implications for GIT-PIX complex assembly
    • Schlenker O, Rittinger K, (2009) Structures of dimeric GIT1 and trimeric beta-PIX and implications for GIT-PIX complex assembly. J Mol Biol 386: 280-289.
    • (2009) J Mol Biol , vol.386 , pp. 280-289
    • Schlenker, O.1    Rittinger, K.2
  • 6
    • 0033577810 scopus 로고    scopus 로고
    • Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: a role in cytoskeletal remodeling
    • Turner CE, Brown MC, Perrotta JA, Riedy MC, Nikolopoulos SN, et al. (1999) Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: a role in cytoskeletal remodeling. J Cell Biol 145: 851-863.
    • (1999) J Cell Biol , vol.145 , pp. 851-863
    • Turner, C.E.1    Brown, M.C.2    Perrotta, J.A.3    Riedy, M.C.4    Nikolopoulos, S.N.5
  • 7
    • 49649120467 scopus 로고    scopus 로고
    • GIT1 paxillin-binding domain is a four-helix bundle, and it binds to both paxillin LD2 and LD4 motifs
    • Zhang ZM, Simmerman JA, Guibao CD, Zheng JJ, (2008) GIT1 paxillin-binding domain is a four-helix bundle, and it binds to both paxillin LD2 and LD4 motifs. J Biol Chem 283: 18685-18693.
    • (2008) J Biol Chem , vol.283 , pp. 18685-18693
    • Zhang, Z.M.1    Simmerman, J.A.2    Guibao, C.D.3    Zheng, J.J.4
  • 8
    • 0037336858 scopus 로고    scopus 로고
    • Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting
    • Ko J, Kim S, Valtschanoff JG, Shin H, Lee JR, et al. (2003a) Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting. J Neurosci 23: 1667-1677.
    • (2003) J Neurosci , vol.23 , pp. 1667-1677
    • Ko, J.1    Kim, S.2    Valtschanoff, J.G.3    Shin, H.4    Lee, J.R.5
  • 9
    • 0029019297 scopus 로고
    • The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions
    • Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, et al. (1995) The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions. EMBO J 14: 2827-2838.
    • (1995) EMBO J , vol.14 , pp. 2827-2838
    • Serra-Pagès, C.1    Kedersha, N.L.2    Fazikas, L.3    Medley, Q.4    Debant, A.5
  • 10
    • 0032546658 scopus 로고    scopus 로고
    • Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins
    • Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M, (1998) Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. J Biol Chem 273: 15611-15620.
    • (1998) J Biol Chem , vol.273 , pp. 15611-15620
    • Serra-Pagès, C.1    Medley, Q.G.2    Tang, M.3    Hart, A.4    Streuli, M.5
  • 11
    • 70350366723 scopus 로고    scopus 로고
    • Liprin-α1 promotes cell spreading on the extracellular matrix by affecting the distribution of activated integrins
    • Asperti C, Astro V, Totaro A, Paris S, de Curtis I, (2009) Liprin-α1 promotes cell spreading on the extracellular matrix by affecting the distribution of activated integrins. J Cell Sci 122: 3225-3232.
    • (2009) J Cell Sci , vol.122 , pp. 3225-3232
    • Asperti, C.1    Astro, V.2    Totaro, A.3    Paris, S.4    de Curtis, I.5
  • 12
    • 23044477857 scopus 로고    scopus 로고
    • GIT1 is a scaffold for ERK1/2 activation in focal adhesions
    • Yin G, Zheng Q, Yan C, Berk BC, (2005) GIT1 is a scaffold for ERK1/2 activation in focal adhesions. J Biol Chem 280: 27705-27712.
    • (2005) J Biol Chem , vol.280 , pp. 27705-27712
    • Yin, G.1    Zheng, Q.2    Yan, C.3    Berk, B.C.4
  • 13
    • 33745216502 scopus 로고    scopus 로고
    • Neutrophil directional sensing and superoxide production linked by the GTPase-activating protein Git2
    • Mazaki Y, Hashimoto S, Tsujimura T, Morishige M, Hashimoto A, et al. (2006) Neutrophil directional sensing and superoxide production linked by the GTPase-activating protein Git2. Nat Immunol 7: 724-731.
    • (2006) Nat Immunol , vol.7 , pp. 724-731
    • Mazaki, Y.1    Hashimoto, S.2    Tsujimura, T.3    Morishige, M.4    Hashimoto, A.5
  • 14
    • 73949141711 scopus 로고    scopus 로고
    • Paxillin-kinase-linker tyrosine phosphorylation regulates directional cell migration
    • Yu JA, Deakin NO, Turner CE, (2009) Paxillin-kinase-linker tyrosine phosphorylation regulates directional cell migration. Mol Biol Cell 20: 4706-4719.
    • (2009) Mol Biol Cell , vol.20 , pp. 4706-4719
    • Yu, J.A.1    Deakin, N.O.2    Turner, C.E.3
  • 15
    • 0035040153 scopus 로고    scopus 로고
    • Cell migration: GAPs between membrane traffic and the cytoskeleton
    • de Curtis I, (2001) Cell migration: GAPs between membrane traffic and the cytoskeleton. EMBO Rep 2: 277-281.
    • (2001) EMBO Rep , vol.2 , pp. 277-281
    • de Curtis, I.1
  • 16
    • 0036537895 scopus 로고    scopus 로고
    • GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration
    • Manabe R, Kovalenko M, Webb DJ, Horwitz AR, (2002) GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration. J Cell Sci 115: 1497-1510.
    • (2002) J Cell Sci , vol.115 , pp. 1497-1510
    • Manabe, R.1    Kovalenko, M.2    Webb, D.J.3    Horwitz, A.R.4
  • 17
    • 33646776346 scopus 로고    scopus 로고
    • Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics
    • Nayal A, Webb DJ, Brown CM, Schaefer EM, Vicente-Manzanares M, et al. (2006) Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics. J Cell Biol 173: 587-589.
    • (2006) J Cell Biol , vol.173 , pp. 587-589
    • Nayal, A.1    Webb, D.J.2    Brown, C.M.3    Schaefer, E.M.4    Vicente-Manzanares, M.5
  • 18
    • 17344366888 scopus 로고    scopus 로고
    • An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells
    • Nishiya N, Kiosses WB, Han J, Ginsberg MH, (2005) An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells. Nat Cell Biol 7: 343-352.
    • (2005) Nat Cell Biol , vol.7 , pp. 343-352
    • Nishiya, N.1    Kiosses, W.B.2    Han, J.3    Ginsberg, M.H.4
  • 19
    • 0035694169 scopus 로고    scopus 로고
    • Molecular mechanisms regulating the subcellular localization of p95-APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface
    • Matafora V, Paris S, Dariozzi S, de Curtis I, (2001) Molecular mechanisms regulating the subcellular localization of p95-APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface. J Cell Sci 114: 4509-4520.
    • (2001) J Cell Sci , vol.114 , pp. 4509-4520
    • Matafora, V.1    Paris, S.2    Dariozzi, S.3    de Curtis, I.4
  • 20
    • 21644460380 scopus 로고    scopus 로고
    • Cdc42 controls the polarity of the actin and microtubule cytoskeletons through two distinct signal transduction pathways
    • Cau J, Hall A, (2005) Cdc42 controls the polarity of the actin and microtubule cytoskeletons through two distinct signal transduction pathways. J Cell Sci 118: 2579-2587.
    • (2005) J Cell Sci , vol.118 , pp. 2579-2587
    • Cau, J.1    Hall, A.2
  • 21
    • 33644539533 scopus 로고    scopus 로고
    • Targeting and activation of Rac1 are mediated by the exchange factor beta-Pix
    • ten Klooster JP, Jaffer ZM, Chernoff J, Hordijk PL, (2006) Targeting and activation of Rac1 are mediated by the exchange factor beta-Pix. J Cell Biol 172: 759-769.
    • (2006) J Cell Biol , vol.172 , pp. 759-769
    • ten Klooster, J.P.1    Jaffer, Z.M.2    Chernoff, J.3    Hordijk, P.L.4
  • 22
    • 34047273596 scopus 로고    scopus 로고
    • Inhibitor of growth 4 suppresses cell spreading and cell migration by interacting with a novel binding partner, liprin α1
    • Shen JC, Unoki M, Ythier D, Duperray A, Varticovski L, et al. (2007) Inhibitor of growth 4 suppresses cell spreading and cell migration by interacting with a novel binding partner, liprin α1. Cancer Res 67: 2552-2558.
    • (2007) Cancer Res , vol.67 , pp. 2552-2558
    • Shen, J.C.1    Unoki, M.2    Ythier, D.3    Duperray, A.4    Varticovski, L.5
  • 23
    • 77649236549 scopus 로고    scopus 로고
    • Liprin-alpha1 affects the distribution of low-affinity beta1 integrins and stabilizes their permanence at the cell surface
    • Asperti C, Pettinato E, de Curtis I, (2010) Liprin-alpha1 affects the distribution of low-affinity beta1 integrins and stabilizes their permanence at the cell surface. Exp Cell Res 316: 915-926.
    • (2010) Exp Cell Res , vol.316 , pp. 915-926
    • Asperti, C.1    Pettinato, E.2    de Curtis, I.3
  • 24
    • 79954613016 scopus 로고    scopus 로고
    • Liprin-α1 regulates breast cancer cell invasion by affecting cell motility, invadopodia and extracellular matrix degradation
    • Astro V, Asperti C, Cangi G, Doglioni C, de Curtis I, (2011) Liprin-α1 regulates breast cancer cell invasion by affecting cell motility, invadopodia and extracellular matrix degradation. Oncogene 30: 1841-1849.
    • (2011) Oncogene , vol.30 , pp. 1841-1849
    • Astro, V.1    Asperti, C.2    Cangi, G.3    Doglioni, C.4    de Curtis, I.5
  • 25
    • 78449305490 scopus 로고    scopus 로고
    • Function of liprins in cell motility
    • de Curtis I, (2011) Function of liprins in cell motility. Exp Cell Res 317: 1-8.
    • (2011) Exp Cell Res , vol.317 , pp. 1-8
    • de Curtis, I.1
  • 26
    • 37049020458 scopus 로고    scopus 로고
    • Identification of an intramolecular interaction important for the regulation of GIT1 functions
    • Totaro A, Paris S, Asperti C, de Curtis I, (2007) Identification of an intramolecular interaction important for the regulation of GIT1 functions. Mol Biol Cell 18: 5124-5138.
    • (2007) Mol Biol Cell , vol.18 , pp. 5124-5138
    • Totaro, A.1    Paris, S.2    Asperti, C.3    de Curtis, I.4
  • 27
    • 0142242179 scopus 로고    scopus 로고
    • Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins
    • Ko J, Na M, Kim S, Lee JR, Kim E, (2003b) Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins. J Biol Chem 278: 42377-42385.
    • (2003) J Biol Chem , vol.278 , pp. 42377-42385
    • Ko, J.1    Na, M.2    Kim, S.3    Lee, J.R.4    Kim, E.5
  • 28
    • 34250656135 scopus 로고    scopus 로고
    • GIT1 utilizes a focal adhesion targeting-homology domain to bind paxillin
    • Schmalzigaug R, Garron ML, Roseman JT, Xing Y, Davidson CE, et al. (2007) GIT1 utilizes a focal adhesion targeting-homology domain to bind paxillin. Cell Signal 19: 1733-1744.
    • (2007) Cell Signal , vol.19 , pp. 1733-1744
    • Schmalzigaug, R.1    Garron, M.L.2    Roseman, J.T.3    Xing, Y.4    Davidson, C.E.5
  • 29
    • 33646566846 scopus 로고    scopus 로고
    • GIT2 represses Crk- and Rac1-regulated cell spreading and Cdc42-mediated focal adhesion turnover
    • Frank SR, Adelstein MR, Hansen SH, (2006) GIT2 represses Crk- and Rac1-regulated cell spreading and Cdc42-mediated focal adhesion turnover. EMBO J 25: 1848-1859.
    • (2006) EMBO J , vol.25 , pp. 1848-1859
    • Frank, S.R.1    Adelstein, M.R.2    Hansen, S.H.3
  • 30
    • 0032894575 scopus 로고    scopus 로고
    • A cell-free system to study regulation of focal adhesions and of the connected actin cytoskeleton
    • Cattelino A, Albertinazzi C, Bossi M, Critchley DR, de Curtis I, (1999) A cell-free system to study regulation of focal adhesions and of the connected actin cytoskeleton. Mol Biol Cell 10: 373-391.
    • (1999) Mol Biol Cell , vol.10 , pp. 373-391
    • Cattelino, A.1    Albertinazzi, C.2    Bossi, M.3    Critchley, D.R.4    de Curtis, I.5
  • 31
    • 33748312025 scopus 로고    scopus 로고
    • ArfGAP family proteins in cell adhesion, migration and tumor invasion
    • Sabe H, Onodera Y, Mazaki Y, Hashimoto S, (2006) ArfGAP family proteins in cell adhesion, migration and tumor invasion. Curr Opin Cell Biol 18: 558-564.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 558-564
    • Sabe, H.1    Onodera, Y.2    Mazaki, Y.3    Hashimoto, S.4
  • 32
    • 76449101129 scopus 로고    scopus 로고
    • The GIT-PIX complexes regulate the chemotactic response of rat basophilic leukaemia cells
    • Gavina M, Za L, Molteni R, Pardi R, de Curtis I, (2010) The GIT-PIX complexes regulate the chemotactic response of rat basophilic leukaemia cells. Biol Cell 102: 231-244.
    • (2010) Biol Cell , vol.102 , pp. 231-244
    • Gavina, M.1    Za, L.2    Molteni, R.3    Pardi, R.4    de Curtis, I.5
  • 33
  • 34
    • 33745333951 scopus 로고    scopus 로고
    • Phosphorylation of serine 709 in GIT1 regulates protrusive activity in cells
    • Webb DJ, Kovalenko M, Whitmore L, Horwitz AF, (2006) Phosphorylation of serine 709 in GIT1 regulates protrusive activity in cells. Biochem Biophys Res Commun 346: 1284-1288.
    • (2006) Biochem Biophys Res Commun , vol.346 , pp. 1284-1288
    • Webb, D.J.1    Kovalenko, M.2    Whitmore, L.3    Horwitz, A.F.4
  • 35
    • 41649110901 scopus 로고    scopus 로고
    • Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy
    • Digman MA, Brown CM, Horwitz AF, Mantulin WW, Gratton E, (2007) Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy. Biophys J 94: 2819-2831.
    • (2007) Biophys J , vol.94 , pp. 2819-2831
    • Digman, M.A.1    Brown, C.M.2    Horwitz, A.F.3    Mantulin, W.W.4    Gratton, E.5
  • 36
    • 1642586962 scopus 로고    scopus 로고
    • FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
    • Webb DJ, Donais K, Whitmore LA, Thomas SM, Turner CE, et al. (2004) FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat Cell Biol 6: 154-161.
    • (2004) Nat Cell Biol , vol.6 , pp. 154-161
    • Webb, D.J.1    Donais, K.2    Whitmore, L.A.3    Thomas, S.M.4    Turner, C.E.5
  • 37
    • 0027421094 scopus 로고
    • A monoclonal antibody against an activation epitope on mouse integrin chain beta 1 blocks adhesion of lymphocytes to the endothelial integrin alpha 6 beta 1
    • Lenter M, Uhlig H, Hamann A, Jenö P, Imhof B, et al. (1993) A monoclonal antibody against an activation epitope on mouse integrin chain beta 1 blocks adhesion of lymphocytes to the endothelial integrin alpha 6 beta 1. Proc Natl Acad Sci USA 90: 9051-9055.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9051-9055
    • Lenter, M.1    Uhlig, H.2    Hamann, A.3    Jenö, P.4    Imhof, B.5
  • 38
    • 0038338507 scopus 로고    scopus 로고
    • Leucine-zipper-mediated homo- and hetero-dimerization of GIT family p95-ARF GTPase-activating protein, PIX-, paxillin-interacting proteins 1 and 2
    • Paris S, Longhi R, Santambrogio P, de Curtis I, (2003) Leucine-zipper-mediated homo- and hetero-dimerization of GIT family p95-ARF GTPase-activating protein, PIX-, paxillin-interacting proteins 1 and 2. Biochem J 372: 391-398.
    • (2003) Biochem J , vol.372 , pp. 391-398
    • Paris, S.1    Longhi, R.2    Santambrogio, P.3    de Curtis, I.4
  • 39
    • 33746885441 scopus 로고    scopus 로고
    • BetaPIX controls cell motility and neurite extension by regulating the distribution of GIT1
    • Za L, Albertinazzi C, Paris S, Gagliani M, Tacchetti C, et al. (2006) BetaPIX controls cell motility and neurite extension by regulating the distribution of GIT1. J Cell Sci 119: 2654-2666.
    • (2006) J Cell Sci , vol.119 , pp. 2654-2666
    • Za, L.1    Albertinazzi, C.2    Paris, S.3    Gagliani, M.4    Tacchetti, C.5
  • 40
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M, (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68: 850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 41
    • 0034213595 scopus 로고    scopus 로고
    • ProFound: an expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang W, Chait BT, (2000) ProFound: an expert system for protein identification using mass spectrometric peptide mapping information. Anal Chem 72: 2482-2489.
    • (2000) Anal Chem , vol.72 , pp. 2482-2489
    • Zhang, W.1    Chait, B.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.