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Volumn 377, Issue 2, 2004, Pages 449-457

A membrane proximal region of the integrin α5 subunit is important for its interaction with nischarin

Author keywords

Biacore; Integrin; Migration; Nischarin; Yeast two hybrid

Indexed keywords

BIOCHEMISTRY; CELL IMMOBILIZATION; CELL MEMBRANES; MUTAGENESIS; SURFACE PLASMON RESONANCE;

EID: 0942290434     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030411     Document Type: Article
Times cited : (31)

References (44)
  • 2
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G. and Ruoslahli, E. (1999) Integrin signaling. Science 285, 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahli, E.2
  • 3
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • Juliano, R. L. (2002) Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu. Rev. Pharmacol. Toxicol. 42, 283-323
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 4
    • 0028238346 scopus 로고
    • Disruption of integrin function and induction of lyrosine phosphorylation by the autonomously expressed β1 integrin cytoplasmic domain
    • Lukashev, M. E., Sheppard, D. and Pytela, R. (1994) Disruption of integrin function and induction of lyrosine phosphorylation by the autonomously expressed β1 integrin cytoplasmic domain. J. Biol. Chem. 269, 18311-18314
    • (1994) J. Biol. Chem. , vol.269 , pp. 18311-18314
    • Lukashev, M.E.1    Sheppard, D.2    Pytela, R.3
  • 5
    • 0034739854 scopus 로고    scopus 로고
    • Activated R-ras, Rac1, PI 3-kinase and PKCε can each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains
    • Berrier. A. L., Mastrangelo, A. M., Downward, J., Ginsberg, M. and LaFlamme, S. E. (2000) Activated R-ras, Rac1, PI 3-kinase and PKCε can each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains. J. Cell Biol. 151, 1549-1560
    • (2000) J. Cell Biol. , vol.151 , pp. 1549-1560
    • Berrier, A.L.1    Mastrangelo, A.M.2    Downward, J.3    Ginsberg, M.4    LaFlamme, S.E.5
  • 6
    • 0030613632 scopus 로고    scopus 로고
    • The αvβ3 integrin regulates α5β1-mediated cell migration toward fibronectin
    • Simon, K. O., Nutt, E. M., Abraham, D. G., Rodan, G. A. and Duong, L. T. (1997) The αvβ3 integrin regulates α5β1-mediated cell migration toward fibronectin. J. Biol. Chem. 272, 29380-29389
    • (1997) J. Biol. Chem. , vol.272 , pp. 29380-29389
    • Simon, K.O.1    Nutt, E.M.2    Abraham, D.G.3    Rodan, G.A.4    Duong, L.T.5
  • 7
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-a antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin α subunits
    • Rojiani, M. V, Finlay, B. B., Gray, V. and Dedhar, S. (1991) In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin α subunits. Biochemistry 30, 9859-9866
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 8
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulalion of expression of calreticulin, an intracellular integrin α-subunit-binding protein
    • Leung-Hagesleijn, C. Y., Milankov, K., Michalak, M., Wilkins, J. and Dedhar, S. (1994) Cell attachment to extracellular matrix substrates is inhibited upon downregulalion of expression of calreticulin, an intracellular integrin α-subunit-binding protein. J. Cell Sci. 107, 589-600
    • (1994) J. Cell Sci. , vol.107 , pp. 589-600
    • Leung-Hagesleijn, C.Y.1    Milankov, K.2    Michalak, M.3    Wilkins, J.4    Dedhar, S.5
  • 9
    • 0034629578 scopus 로고    scopus 로고
    • The cytoplasmic domain of the α1 integrin subunit influences stress fiber formation via the conserved GFFKR motif
    • Vossmeyer, D., Kaufmann, C., Loster, K., Lucka, L., Horstkorte, R., Reutter, W. and Danker, K. (2000) The cytoplasmic domain of the α1 integrin subunit influences stress fiber formation via the conserved GFFKR motif. Exp. Cell Res. 256, 321-327
    • (2000) Exp. Cell Res. , vol.256 , pp. 321-327
    • Vossmeyer, D.1    Kaufmann, C.2    Loster, K.3    Lucka, L.4    Horstkorte, R.5    Reutter, W.6    Danker, K.7
  • 10
    • 0035167613 scopus 로고    scopus 로고
    • The cytoplasmic domain of the integrin α9 subunit requires the adaptor protein paxillin to inhibit cell spreading but promotes cell migration in a paxillin-independent manner
    • Young, B. A., Taooka, Y., Liu, S., Askins, K. J., Yokosaki, Y., Thomas, S. M. and Sheppard, D. (2001) The cytoplasmic domain of the integrin α9 subunit requires the adaptor protein paxillin to inhibit cell spreading but promotes cell migration in a paxillin-independent manner. Mol. Biol. Cell 12, 3214-3225
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3214-3225
    • Young, B.A.1    Taooka, Y.2    Liu, S.3    Askins, K.J.4    Yokosaki, Y.5    Thomas, S.M.6    Sheppard, D.7
  • 11
    • 0028971037 scopus 로고
    • β3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin β3 subunit
    • Shattil, S. J., O'Toole, T., Eigenthaler, M., Thon, V., Williams, M., Babior, B. M. and Ginsberg, M. H. (1995) β3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin β3 subunit. J. Cell Biol. 131, 807-816
    • (1995) J. Cell Biol. , vol.131 , pp. 807-816
    • Shattil, S.J.1    O'Toole, T.2    Eigenthaler, M.3    Thon, V.4    Williams, M.5    Babior, B.M.6    Ginsberg, M.H.7
  • 13
    • 0030602819 scopus 로고    scopus 로고
    • α L β2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
    • Kolanus, W., Nagel, W., Schiller, B., Zeitlmann, L., Godar, S., Stockinger, H. and Seed, B. (1996) α L β2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell 86, 233-242
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1    Nagel, W.2    Schiller, B.3    Zeitlmann, L.4    Godar, S.5    Stockinger, H.6    Seed, B.7
  • 14
    • 0031046185 scopus 로고    scopus 로고
    • Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain
    • Naik, U. P., Patel, P. M. and Parise, L. V. (1997) Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain. J. Biol. Chem. 272, 4651-4654
    • (1997) J. Biol. Chem. , vol.272 , pp. 4651-4654
    • Naik, U.P.1    Patel, P.M.2    Parise, L.V.3
  • 15
    • 0030040067 scopus 로고    scopus 로고
    • Direct binding of the platelet integrin αIIbβ3 (GPIIb-IIIa) to talin. Evidence that interaction is mediated through the cytoplasmic domains of both αIIb and β3
    • Knezevic, I., Leisner, T. M. and Lam, S. C. (1996) Direct binding of the platelet integrin αIIbβ3 (GPIIb-IIIa) to talin. Evidence that interaction is mediated through the cytoplasmic domains of both αIIb and β3. J. Biol. Chem. 271, 16416-16421
    • (1996) J. Biol. Chem. , vol.271 , pp. 16416-16421
    • Knezevic, I.1    Leisner, T.M.2    Lam, S.C.3
  • 16
    • 0037036462 scopus 로고    scopus 로고
    • A fragment of paxillin binds the α 4 integrin cytoplasmic domain (tail) and selectively inhibits α 4-mediated cell migration
    • Liu, S., Kiosses, W. B., Rose, D. M., Slepak, M., Salgia, R., Griffin, J. D., Turner, C. E., Schwartz, M. A. and Ginsberg, M. H. (2002) A fragment of paxillin binds the α 4 integrin cytoplasmic domain (tail) and selectively inhibits α 4-mediated cell migration. J. Biol. Chem. 277, 20887-20894
    • (2002) J. Biol. Chem. , vol.277 , pp. 20887-20894
    • Liu, S.1    Kiosses, W.B.2    Rose, D.M.3    Slepak, M.4    Salgia, R.5    Griffin, J.D.6    Turner, C.E.7    Schwartz, M.A.8    Ginsberg, M.H.9
  • 17
    • 0034638831 scopus 로고    scopus 로고
    • Nischarin, a novel protein that interacts with the integrin α5 subunit and inhibits cell migration
    • Alahari, S. K., Lee, J. W. and Juliano, R. L. (2000) Nischarin, a novel protein that interacts with the integrin α5 subunit and inhibits cell migration. J. Cell Biol. 151, 1141-1154
    • (2000) J. Cell Biol. , vol.151 , pp. 1141-1154
    • Alahari, S.K.1    Lee, J.W.2    Juliano, R.L.3
  • 18
    • 0042564472 scopus 로고    scopus 로고
    • Nischarin inhibits Rac induced migration and invasion of epithelial cells by affecting signaling cascades involving PAK
    • Alahari, S. K. (2003) Nischarin inhibits Rac induced migration and invasion of epithelial cells by affecting signaling cascades involving PAK. Exp. Cell Res. 288, 415-424
    • (2003) Exp. Cell Res. , vol.288 , pp. 415-424
    • Alahari, S.K.1
  • 19
    • 0035800830 scopus 로고    scopus 로고
    • RGS12 and RGS14 GoLoco motifs are G α(i) interaction sites with guanine nucleotide dissociation inhibitor activity
    • Kimple, R. J., De Vries, L., Tronchere, H., Behe, C. I., Morris, R. A., Gist Farquhar, M. and Siderovski, D. P. (2001) RGS12 and RGS14 GoLoco motifs are G α(i) interaction sites with guanine nucleotide dissociation inhibitor activity. J. Biol. Chem. 276, 29275-29281
    • (2001) J. Biol. Chem. , vol.276 , pp. 29275-29281
    • Kimple, R.J.1    De Vries, L.2    Tronchere, H.3    Behe, C.I.4    Morris, R.A.5    Gist Farquhar, M.6    Siderovski, D.P.7
  • 20
    • 0035920245 scopus 로고    scopus 로고
    • BIAcore analysis of bovine insulin-like growth factor (IGF)-binding protein-2 identifies major IGF binding site determinants in both the amino- And carboxyl-terminal domains
    • Carrick, F. E., Forbes, B. E. and Wallace, J. C. (2001) BIAcore analysis of bovine insulin-like growth factor (IGF)-binding protein-2 identifies major IGF binding site determinants in both the amino-and carboxyl-terminal domains. J. Biol. Chem. 276, 27120-27128
    • (2001) J. Biol. Chem. , vol.276 , pp. 27120-27128
    • Carrick, F.E.1    Forbes, B.E.2    Wallace, J.C.3
  • 22
    • 0033601259 scopus 로고    scopus 로고
    • Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits
    • Armulik, A, Nilsson, I., von Heijne, G. and Johansson, S. (1999) Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits. J. Biol. Chem. 274, 37030-37034
    • (1999) J. Biol. Chem. , vol.274 , pp. 37030-37034
    • Armulik, A.1    Nilsson, I.2    Von Heijne, G.3    Johansson, S.4
  • 23
    • 0034176183 scopus 로고    scopus 로고
    • Electrostatic interactions affecting the active site of class sigma glutathione S-transferase
    • Stevens, J. M., Armstrong, R. N. and Dirr, H. W. (2000) Electrostatic interactions affecting the active site of class sigma glutathione S-transferase. Biochem. J. 347, 193-197
    • (2000) Biochem. J. , vol.347 , pp. 193-197
    • Stevens, J.M.1    Armstrong, R.N.2    Dirr, H.W.3
  • 24
    • 2242443511 scopus 로고    scopus 로고
    • Molecular recognition at the dimer interface of a class μ glutathione transferase: Role of a hydrophobic interaction motif in dimer stability and protein function
    • Hornby, J. A., Codreanu, S. G., Armstrong, R. N. and Dirr, H. W. (2002) Molecular recognition at the dimer interface of a class μ glutathione transferase: role of a hydrophobic interaction motif in dimer stability and protein function. Biochemistry 41, 14238-14247
    • (2002) Biochemistry , vol.41 , pp. 14238-14247
    • Hornby, J.A.1    Codreanu, S.G.2    Armstrong, R.N.3    Dirr, H.W.4
  • 25
    • 0030842771 scopus 로고    scopus 로고
    • Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli
    • Tudyka, T. and Skerra, A. (1997) Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci. 6, 2180-2187
    • (1997) Protein Sci. , vol.6 , pp. 2180-2187
    • Tudyka, T.1    Skerra, A.2
  • 27
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov, P. L. and Gill, S. J. (1988) Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39, 191-234
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 28
    • 0038352023 scopus 로고    scopus 로고
    • Thermodynamic analysis of the increased stability of major histocompatibility complex class II molecule I-Ek complexed with an antigenic peptide at an acidic pH
    • Saito, K., Sarai, A., Oda, M., Azuma, T. and Kozono, H. (2003) Thermodynamic analysis of the increased stability of major histocompatibility complex class II molecule I-Ek complexed with an antigenic peptide at an acidic pH. J. Biol. Chem. 278, 14732-14738
    • (2003) J. Biol. Chem. , vol.278 , pp. 14732-14738
    • Saito, K.1    Sarai, A.2    Oda, M.3    Azuma, T.4    Kozono, H.5
  • 29
    • 0016712926 scopus 로고
    • Effects of proteins on thermotropic phase transitions of phospholipid membranes
    • Papahadjopoulos, D., Moscarello, M., Eylar, E. H. and Isac, T. (1975) Effects of proteins on thermotropic phase transitions of phospholipid membranes. Biochim. Biophys. Acta 401, 317-335
    • (1975) Biochim. Biophys. Acta , vol.401 , pp. 317-335
    • Papahadjopoulos, D.1    Moscarello, M.2    Eylar, E.H.3    Isac, T.4
  • 31
    • 0033214440 scopus 로고    scopus 로고
    • Identification of a talin-binding site in the integrin β(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin N-terminal head domain interacts with the membrane-proximal region of the β(3) cytoplasmic tail
    • Patil, S., Jedsadayanmata, A., Wencel-Drake, J. D., Wang, W., Knezevic, I. and Lam, S. C. (1999) Identification of a talin-binding site in the integrin β(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin N-terminal head domain interacts with the membrane-proximal region of the β(3) cytoplasmic tail. J. Biol. Chem. 274, 28575-28583
    • (1999) J. Biol. Chem. , vol.274 , pp. 28575-28583
    • Patil, S.1    Jedsadayanmata, A.2    Wencel-Drake, J.D.3    Wang, W.4    Knezevic, I.5    Lam, S.C.6
  • 33
    • 0038503260 scopus 로고    scopus 로고
    • Domain-specific interactions of talin with the membrane-proximal region of the integrin β3 subunit
    • Ulmer, T. S., Calderwood, D. A., Ginsberg, M. H. and Campbell, I. D. (2003) Domain-specific interactions of talin with the membrane-proximal region of the integrin β3 subunit. Biochemistry 42, 8307-6312
    • (2003) Biochemistry , vol.42 , pp. 8307-16312
    • Ulmer, T.S.1    Calderwood, D.A.2    Ginsberg, M.H.3    Campbell, I.D.4
  • 35
    • 0026331047 scopus 로고
    • Modulation of the affinity of integrin αIIb/βIIIa by the cytoplasmic domain of αIIb
    • O'Toole, T. E., Mandelman, D., Forsyth, J., Shattil, S. J., Plow, E. F. and Ginsberg, M. H. (1991) Modulation of the affinity of integrin αIIb/βIIIa by the cytoplasmic domain of αIIb. Science 254, 845-847
    • (1991) Science , vol.254 , pp. 845-847
    • O'Toole, T.E.1    Mandelman, D.2    Forsyth, J.3    Shattil, S.J.4    Plow, E.F.5    Ginsberg, M.H.6
  • 38
    • 0037040929 scopus 로고    scopus 로고
    • Molecular basis for interaction between Icap1 α PTB domain and β 1 integrin
    • Chang, D. D., Hoang, B. Q., Liu, J. and Springer, T. A. (2002) Molecular basis for interaction between Icap1 α PTB domain and β 1 integrin. J. Biol. Chem. 277, 8140-8145
    • (2002) J. Biol. Chem. , vol.277 , pp. 8140-8145
    • Chang, D.D.1    Hoang, B.Q.2    Liu, J.3    Springer, T.A.4
  • 39
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes, P. E., O'Toole, T. E., Ylanne, J., Shattil, S. J. and Ginsberg, M. H. (1995) The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J. Biol. Chem. 270, 12411-12417
    • (1995) J. Biol. Chem. , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 40
    • 0029966310 scopus 로고    scopus 로고
    • Breaking the integrin hinge. A defined structural constraint regulates integrin signaling
    • Hughes, P. E., Diaz-Gonzalez, F., Leong, L., Wu, C., McDonald, J. A. and Shattil, S. J. (1996) Breaking the integrin hinge. A defined structural constraint regulates integrin signaling. J. Biol. Chem. 271, 6571-6574
    • (1996) J. Biol. Chem. , vol.271 , pp. 6571-6574
    • Hughes, P.E.1    Diaz-Gonzalez, F.2    Leong, L.3    Wu, C.4    McDonald, J.A.5    Shattil, S.J.6
  • 41
    • 0033546169 scopus 로고    scopus 로고
    • Divalent cations differentially regulate integrin αIIb cytoplasmic tail binding to β3 and to calcium- and integrin-binding protein
    • Vallar, L., Melchior, C., Plancon, S., Drobecq, H., Lippens, G., Regnault, V. and Kieffer, N. (1999) Divalent cations differentially regulate integrin αIIb cytoplasmic tail binding to β3 and to calcium-and integrin-binding protein. J. Biol. Chem. 274, 17257-17266
    • (1999) J. Biol. Chem. , vol.274 , pp. 17257-17266
    • Vallar, L.1    Melchior, C.2    Plancon, S.3    Drobecq, H.4    Lippens, G.5    Regnault, V.6    Kieffer, N.7
  • 43
    • 0030924021 scopus 로고    scopus 로고
    • ICAP-1, a novel β1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of β1 integrin
    • Chang, D. D., Wong, C., Smith, H. and Liu, J. (1997) ICAP-1, a novel β1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of β1 integrin. J. Cell Biol. 138, 1149-1157
    • (1997) J. Cell Biol. , vol.138 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 44
    • 0032590074 scopus 로고    scopus 로고
    • Interaction of the integrin β1 cytoplasmic domain with ICAP-1 protein
    • Zhang, X. A. and Hemler, M. E. (1999) Interaction of the integrin β1 cytoplasmic domain with ICAP-1 protein, J. Biol. Chem. 274, 11-19
    • (1999) J. Biol. Chem. , vol.274 , pp. 11-19
    • Zhang, X.A.1    Hemler, M.E.2


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