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Volumn 288, Issue 28, 2013, Pages 20248-20260

Calcium and calmodulin-dependent serine/threonine protein kinase type II (CaMKII)-mediated intramolecular opening of integrin cytoplasmic domain-associated protein-1 (ICAP-1α) negatively regulates β1 integrins

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL DOMAINS; CYTOPLASMIC DOMAINS; DIRECT INTERACTIONS; FOCAL ADHESION ASSEMBLY; INTEGRIN ACTIVATION; INTEGRIN AFFINITY; INTRAMOLECULAR INTERACTIONS; MOLECULAR MECHANISM;

EID: 84880075455     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.455956     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins. Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002) Integrins. Bidirectional, allosteric signaling machines. Cell 110, 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • DOI 10.1016/S0092-8674(00)81280-5
    • Lauffenburger, D. A., and Horwitz, A. F. (1996) Cell migration. A physically integrated molecular process. Cell 84, 359-369 (Pubitemid 26058561)
    • (1996) Cell , vol.84 , Issue.3 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 5
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational earrangements in integrin extracellular domains in outside-in and inside-out signaling
    • DOI 10.1016/S0092-8674(02)00935-2
    • Takagi, J., Petre, B. M., Walz, T., and Springer, T. A. (2002) Global conformational rearrangements in integrin extracellular domains in out-side- in and inside-out signaling. Cell 110, 599-611 (Pubitemid 35247840)
    • (2002) Cell , vol.110 , Issue.5 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 6
    • 4444281827 scopus 로고    scopus 로고
    • Regulation of integrin function through conformational complexity: Not simply a knee-jerk reaction?
    • DOI 10.1016/j.ceb.2004.07.003, PII S0955067404000985
    • Mould, A. P., and Humphries, M. J. (2004) Regulation of integrin function through conformational complexity. Not simply a knee-jerk reaction? Curr. Opin. Cell Biol. 16, 544-551 (Pubitemid 39201239)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.5 , pp. 544-551
    • Mould, A.P.1    Humphries, M.J.2
  • 8
    • 44449148944 scopus 로고    scopus 로고
    • The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate β1 and β3 integrins
    • Bouaouina, M., Lad, Y., and Calderwood, D. A. (2008) The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate β1 and β3 integrins. J. Biol. Chem. 283, 6118-6125
    • (2008) J. Biol. Chem. , vol.283 , pp. 6118-6125
    • Bouaouina, M.1    Lad, Y.2    Calderwood, D.A.3
  • 9
    • 1342346591 scopus 로고    scopus 로고
    • The Kindler Syndrome Protein Is Regulated by Transforming Growth Factor-β and Involved in Integrin-mediated Adhesion
    • DOI 10.1074/jbc.M307978200
    • Kloeker, S., Major, M. B., Calderwood, D. A., Ginsberg, M. H., Jones, D. A., and Beckerle, M. C. (2004) The Kindler syndrome protein is regulated by transforming growth factor-β and involved in integrin-mediated adhesion. J. Biol. Chem. 279, 6824-6833 (Pubitemid 38248824)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6824-6833
    • Kloeker, S.1    Major, M.B.2    Calderwood, D.A.3    Ginsberg, M.H.4    Jones, D.A.5    Beckerle, M.C.6
  • 10
    • 34547120497 scopus 로고    scopus 로고
    • The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility
    • DOI 10.1074/jbc.M611680200
    • Shi, X., Ma, Y. Q., Tu, Y., Chen, K., Wu, S., Fukuda, K., Qin, J., Plow, E. F., and Wu, C. (2007) The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility. J. Biol. Chem. 282, 20455-20466 (Pubitemid 47100027)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20455-20466
    • Shi, X.1    Ma, Y.-Q.2    Tu, Y.3    Chen, K.4    Wu, S.5    Fukuda, K.6    Qin, J.7    Plow, E.F.8    Wu, C.9
  • 12
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser, M., Legate, K. R., Zent, R., and Fässler, R. (2009) The tail of integrins, talin, and kindlins. Science 324, 895-899
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fässler, R.4
  • 13
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • DOI 10.1038/nm1722, PII NM1722
    • Moser, M., Nieswandt, B., Ussar, S., Pozgajova, M., and Fässler, R. (2008) Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 14, 325-330 (Pubitemid 351347914)
    • (2008) Nature Medicine , vol.14 , Issue.3 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 16
    • 34547731529 scopus 로고    scopus 로고
    • Defective osteoblast function in ICAP-1-deficient mice
    • DOI 10.1242/dev.000877
    • Bouvard, D., Aszodi, A., Kostka, G., Block, M. R., Albigès-Rizo, C., and Fässler, R. (2007) Defective osteoblast function in ICAP-1-deficient mice. Development 134, 2615-2625 (Pubitemid 47225958)
    • (2007) Development , vol.134 , Issue.14 , pp. 2615-2625
    • Bouvard, D.1    Aszodi, A.2    Kostka, G.3    Block, M.R.4    Albiges-Rizo, C.5    Fassler, R.6
  • 18
    • 0030924021 scopus 로고    scopus 로고
    • 1 integrin
    • DOI 10.1083/jcb.138.5.1149
    • Chang, D. D., Wong, C., Smith, H., and Liu, J. (1997) ICAP-1, a novel β1integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of β1 integrin. J. Cell Biol. 138, 1149-1157 (Pubitemid 27386463)
    • (1997) Journal of Cell Biology , vol.138 , Issue.5 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 19
    • 0032590074 scopus 로고    scopus 로고
    • 1 cytoplasmic domain with ICAP-1 protein
    • DOI 10.1074/jbc.274.1.11
    • Zhang, X. A., and Hemler, M. E. (1999) Interaction of the integrin β1cytoplasmic domain with ICAP-1 protein. J. Biol. Chem. 274, 11-19 (Pubitemid 29035023)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 11-19
    • Zhang, X.A.1    Hemler, M.E.2
  • 22
    • 46749113528 scopus 로고    scopus 로고
    • CaMK-II promotes focal adhesion turnover and cell motility by inducing tyrosine dephosphorylation of FAK and paxillin
    • Easley, C. A., 4th, Brown, C. M., Horwitz, A. F., and Tombes, R. M. (2008) CaMK-II promotes focal adhesion turnover and cell motility by inducing tyrosine dephosphorylation of FAK and paxillin. Cell Motil. Cytoskeleton 65, 662-674
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 662-674
    • Easley IV, C.A.1    Brown, C.M.2    Horwitz, A.F.3    Tombes, R.M.4
  • 23
    • 0030818837 scopus 로고    scopus 로고
    • 3 integrin complex is reversed by activated calcium/calmodulin-dependent protein kinase II
    • Bilato, C., Curto, K. A., Monticone, R. E., Pauly, R. R., White, A. J., and Crow, M. T. (1997) The inhibition of vascular smooth muscle cell migration by peptide and antibody antagonists of the αvβ3 integrin complex isreversed by activated calcium/calmodulin- dependent protein kinase II. J. Clin. Invest. 100, 693-704 (Pubitemid 27340519)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.3 , pp. 693-704
    • Bilato, C.1    Curto, K.A.2    Monticone, R.E.3    Pauly, R.R.4    White, A.J.5    Crow, M.T.6
  • 24
    • 0032213801 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle migration by mitogen-activated protein kinase and calcium/calmodulin-dependent protein kinase II signaling pathways
    • DOI 10.1006/jmcc.1998.0795
    • Lundberg, M. S., Curto, K. A., Bilato, C., Monticone, R. E., and Crow, M. T. (1998) Regulation of vascular smooth muscle migration by mitogen-activated protein kinase and calcium/calmodulin-dependent protein kinase II signaling pathways. J. Mol. Cell Cardiol. 30, 2377-2389 (Pubitemid 28549988)
    • (1998) Journal of Molecular and Cellular Cardiology , vol.30 , Issue.11 , pp. 2377-2389
    • Lundberg, M.S.1    Curto, K.A.2    Bilato, C.3    Monticone, R.E.4    Crow, M.T.5
  • 25
    • 0033577813 scopus 로고    scopus 로고
    • 1 function
    • DOI 10.1083/jcb.145.4.889
    • Blystone, S. D., Slater, S. E., Williams, M. P., Crow, M. T., and Brown, E. J. (1999) A molecular mechanism of integrin crosstalk. αvβ3 suppression ofcalcium/calmodulin-dependent protein kinase II regulates α5β1 function.J. Cell Biol. 145, 889-897 (Pubitemid 29240863)
    • (1999) Journal of Cell Biology , vol.145 , Issue.4 , pp. 889-897
    • Blystone, S.D.1    Slater, S.E.2    Williams, M.P.3    Crow, M.T.4    Brown, E.J.5
  • 26
    • 0031915053 scopus 로고    scopus 로고
    • 1 integrin-mediated inside-out signaling
    • Bouvard, D., Molla, A., and Block, M. R. (1998) Calcium/calmodulin- dependent protein kinase II controls α5β1 integrin-mediated inside-out signaling.J. Cell Sci. 111, 657-665 (Pubitemid 28142370)
    • (1998) Journal of Cell Science , vol.111 , Issue.5 , pp. 657-665
    • Bouvard, D.1    Molla, A.2    Block, M.R.3
  • 27
    • 0032501044 scopus 로고    scopus 로고
    • 1-mediated cell adhesion through the integrin cytoplasmic domain associated protein-1α
    • DOI 10.1006/bbrc.1998.9592
    • Bouvard, D., and Block, M. R. (1998) Calcium/calmodulin-dependent protein kinase II controls integrin α5β1-mediated cell adhesion through theintegrin cytoplasmic domain associated protein-1α. Biochem. Biophys. Res. Commun. 252, 46-50 (Pubitemid 28534625)
    • (1998) Biochemical and Biophysical Research Communications , vol.252 , Issue.1 , pp. 46-50
    • Bouvard, D.1    Block, M.R.2
  • 28
    • 0036663023 scopus 로고    scopus 로고
    • Transgenic calmodulin-dependent protein kinase II activation: Dose-dependent effects on synaptic plasticity, learning, and memory
    • Bejar, R., Yasuda, R., Krugers, H., Hood, K., and Mayford, M. (2002) Transgenic calmodulin-dependent protein kinase II activation. Dose-dependent effects on synaptic plasticity, learning, and memory. J. Neurosci. 22, 5719-5726 (Pubitemid 35386494)
    • (2002) Journal of Neuroscience , vol.22 , Issue.13 , pp. 5719-5726
    • Bejar, R.1    Yasuda, R.2    Krugers, H.3    Hood, K.4    Mayford, M.5
  • 29
    • 0029013598 scopus 로고
    • Impairment of spatial but not contextual memory in CaMKII mutant mice with a selective loss of hippocampal LTP in the range of the θ frequency
    • Bach, M. E., Hawkins, R. D., Osman, M., Kandel, E. R., and Mayford, M. (1995) Impairment of spatial but not contextual memory in CaMKII mutant mice with a selective loss of hippocampal LTP in the range of the θ frequency. Cell 81, 905-915
    • (1995) Cell , vol.81 , pp. 905-915
    • Bach, M.E.1    Hawkins, R.D.2    Osman, M.3    Kandel, E.R.4    Mayford, M.5
  • 30
    • 0030476713 scopus 로고    scopus 로고
    • Mice expressing activated CaMKII lack low frequency LTP and do not form stable place cells in the CA1 region of the hippocampus
    • DOI 10.1016/S0092-8674(00)81829-2
    • Rotenberg, A., Mayford, M., Hawkins, R. D., Kandel, E. R., and Muller, R. U. (1996) Mice expressing activated CaMKII lack low frequency LTP and do not form stable place cells in the CA1 region of the hippocampus. Cell 87, 1351-1361 (Pubitemid 27010117)
    • (1996) Cell , vol.87 , Issue.7 , pp. 1351-1361
    • Rotenberg, A.1    Mayford, M.2    Hawkins, R.D.3    Kandel, E.R.4    Muller, R.U.5
  • 31
    • 0035945353 scopus 로고    scopus 로고
    • Marching at the front and dragging behind: Differential αVβ3-integrin turnover regulates focal adhesion behavior
    • DOI 10.1083/jcb.200107107
    • Ballestrem, C., Hinz, B., Imhof, B. A., and Wehrle-Haller, B. (2001) Marching at the front and dragging behind. Differential αVβ3-integrin turnoverregulates focal adhesion behavior. J. Cell Biol. 155, 1319-1332 (Pubitemid 34286280)
    • (2001) Journal of Cell Biology , vol.155 , Issue.7 , pp. 1319-1332
    • Ballestrem, C.1    Hinz, B.2    Imhof, B.A.3    Wehrle-Haller, B.4
  • 33
    • 0037148525 scopus 로고    scopus 로고
    • The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading
    • DOI 10.1083/jcb.200108030
    • Degani, S., Balzac, F., Brancaccio, M., Guazzone, S., Retta, S. F., Silengo, L., Eva, A., and Tarone, G. (2002) The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading. J. Cell Biol. 156, 377-387 (Pubitemid 34839917)
    • (2002) Journal of Cell Biology , vol.156 , Issue.2 , pp. 377-387
    • Degani, S.1    Balzac, F.2    Brancaccio, M.3    Guazzone, S.4    Retta, S.F.5    Silengo, L.6    Eva, A.7    Tarone, G.8
  • 34
    • 84874277570 scopus 로고    scopus 로고
    • Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation
    • Liu, W., Draheim, K. M., Zhang, R., Calderwood, D. A., and Boggon, T. J. (2013) Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation. Mol. Cell 49, 719-729
    • (2013) Mol. Cell , vol.49 , pp. 719-729
    • Liu, W.1    Draheim, K.M.2    Zhang, R.3    Calderwood, D.A.4    Boggon, T.J.5
  • 35
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson, R. P., and Craig, S. W. (1994) An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 269, 12611-12619 (Pubitemid 24202049)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.17 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 36
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R. P., and Craig, S. W. (1995) F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373, 261-264
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 37
    • 46149093439 scopus 로고    scopus 로고
    • Structural Basis for the Autoinhibition of Talin in Regulating Integrin Activation
    • DOI 10.1016/j.molcel.2008.06.011, PII S1097276508004292
    • Goksoy, E., Ma, Y. Q., Wang, X., Kong, X., Perera, D., Plow, E. F., and Qin, J. (2008) Structural basis for the autoinhibition of talin in regulating integrin activation. Mol. Cell 31, 124-133 (Pubitemid 351905930)
    • (2008) Molecular Cell , vol.31 , Issue.1 , pp. 124-133
    • Goksoy, E.1    Ma, Y.-Q.2    Wang, X.3    Kong, X.4    Perera, D.5    Plow, E.F.6    Qin, J.7
  • 39
    • 0029609581 scopus 로고
    • Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains
    • DOI 10.1021/bi00051a034
    • Bretscher, A., Gary, R., and Berryman, M. (1995) Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains. Biochemistry 34, 16830-16837 (Pubitemid 26011808)
    • (1995) Biochemistry , vol.34 , Issue.51 , pp. 16830-16837
    • Bretscher, A.1    Gary, R.2    Berryman, M.3
  • 40
    • 0028987905 scopus 로고
    • EzrinNH2-terminal domain inhibits the cell extensionactivity of the COOH-terminal domain
    • Martin, M., Andréoli, C., Sahuquet, A., Montcourrier, P., Algrain, M., and Mangeat, P. (1995) EzrinNH2-terminal domain inhibits the cell extensionactivity of the COOH-terminal domain. J. Cell Biol. 128, 1081-1093
    • (1995) J. Cell Biol. , vol.128 , pp. 1081-1093
    • Martin, M.1    Andréoli, C.2    Sahuquet, A.3    Montcourrier, P.4    Algrain, M.5    Mangeat, P.6
  • 42
    • 84863161750 scopus 로고    scopus 로고
    • Phosphorylation sites in the cerebral cavernous malformations complex
    • Kim, J., Sherman, N. E., Fox, J. W., and Ginsberg, M. H. (2011) Phosphorylation sites in the cerebral cavernous malformations complex. J. Cell Sci. 124, 3929-3932
    • (2011) J. Cell Sci. , vol.124 , pp. 3929-3932
    • Kim, J.1    Sherman, N.E.2    Fox, J.W.3    Ginsberg, M.H.4
  • 46
    • 0030035971 scopus 로고    scopus 로고
    • 3- and store-independent calcium influx
    • Sjaastad, M. D., Lewis, R. S., and Nelson, W. J. (1996) Mechanisms of integrin-mediated calcium signaling in MDCK cells. Regulation of adhesion by IP3- and store-independent calcium influx. Mol. Biol. Cell 7, 1025-1041 (Pubitemid 26244201)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.7 , pp. 1025-1041
    • Sjaastad, M.D.1    Lewis, R.S.2    Nelson, W.J.3
  • 47
    • 47249121386 scopus 로고    scopus 로고
    • CaM kinase II δ2-dependentregulation of vascular smooth muscle cell polarization and migration
    • Mercure, M. Z., Ginnan, R., and Singer, H. A. (2008) CaM kinase II δ2-dependentregulation of vascular smooth muscle cell polarization and migration. Am. J. Physiol. Cell Physiol. 294, C1465-C1475
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294
    • Mercure, M.Z.1    Ginnan, R.2    Singer, H.A.3
  • 48
    • 0037036371 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-associated protein 1α (ICAP-1α) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement
    • DOI 10.1074/jbc.M200200200
    • Fournier, H. N., Dupé-Manet, S., Bouvard, D., Lacombe, M. L., Marie, C., Block, M. R., and Albiges-Rizo, C. (2002) Integrin cytoplasmic domain-associated protein 1α (ICAP-1α) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement. J. Biol. Chem. 277, 20895-20902 (Pubitemid 34967398)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20895-20902
    • Fournier, H.-N.1    Dupe-Manet, S.2    Bouvard, D.3    Lacombe, M.-L.4    Marie, C.5    Block, M.R.6    Albiges-Rizo, C.7
  • 49
    • 0017375736 scopus 로고
    • Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
    • Engvall, E., and Ruoslahti, E. (1977) Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int. J. Cancer 20, 1-5 (Pubitemid 8139735)
    • (1977) International Journal of Cancer , vol.20 , Issue.1 , pp. 1-5
    • Engvall, E.1    Ruoslahti, E.2
  • 50
    • 77951153298 scopus 로고    scopus 로고
    • Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6
    • Humphries, J. D., Byron, A., Bass, M. D., Craig, S. E., Pinney, J. W., Knight, D., and Humphries, M. J. (2009) Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Sci. Signal. 2, ra51 Médicale
    • (2009) Sci. Signal. , vol.2
    • Humphries, J.D.1    Byron, A.2    Bass, M.D.3    Craig, S.E.4    Pinney, J.W.5    Knight, D.6    Humphries, M.J.7


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