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Volumn 364, Issue 3, 2007, Pages 540-548

A NPxY-independent β5 integrin activation signal regulates phagocytosis of apoptotic cells

Author keywords

5 Integrin; Integrin activation; Integrin EGFP fusion proteins; MFG E8; Non conventional integrin activation signals; NPxY motifs; Phagocytosis of apoptotic cell; Talin

Indexed keywords

ALPHAVBETA5 INTEGRIN; BETA5 INTEGRIN; COMPLEMENTARY DNA; ENHANCED GREEN FLUORESCENT PROTEIN; FOCAL ADHESION KINASE; HYBRID PROTEIN; MICROSPHERE; MUTANT PROTEIN; PAXILLIN; TALIN; VITRONECTIN RECEPTOR; BETA INTEGRIN; PROTEIN SUBUNIT;

EID: 35648951623     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.049     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti F.G., and Ruoslahti E. Integrin signaling. Science 285 5430 (1999) 1028-1032
    • (1999) Science , vol.285 , Issue.5430 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 3
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • Liddington R.C., and Ginsberg M.H. Integrin activation takes shape. J. Cell Biol. 158 5 (2002) 833-839
    • (2002) J. Cell Biol. , vol.158 , Issue.5 , pp. 833-839
    • Liddington, R.C.1    Ginsberg, M.H.2
  • 6
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., and Springer T.A. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301 5640 (2003) 1720-1725
    • (2003) Science , vol.301 , Issue.5640 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 7
    • 0029050683 scopus 로고
    • Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo
    • Filardo E.J., Brooks P.C., Deming S.L., Damsky C., and Cheresh D.A. Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo. J. Cell Biol. 130 2 (1995) 441-450
    • (1995) J. Cell Biol. , vol.130 , Issue.2 , pp. 441-450
    • Filardo, E.J.1    Brooks, P.C.2    Deming, S.L.3    Damsky, C.4    Cheresh, D.A.5
  • 8
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 110 6 (2002) 673-687
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 9
    • 0033592610 scopus 로고    scopus 로고
    • Integrin cytoplasmic tyrosine motif is required for outside-in alphaIIbbeta3 signalling and platelet function
    • Law D.A., DeGuzman F.R., Heiser P., Ministri-Madrid K., Killeen N., and Phillips D.R. Integrin cytoplasmic tyrosine motif is required for outside-in alphaIIbbeta3 signalling and platelet function. Nature 401 6755 (1999) 808-811
    • (1999) Nature , vol.401 , Issue.6755 , pp. 808-811
    • Law, D.A.1    DeGuzman, F.R.2    Heiser, P.3    Ministri-Madrid, K.4    Killeen, N.5    Phillips, D.R.6
  • 10
    • 34147140579 scopus 로고    scopus 로고
    • Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets
    • Zou Z., Chen H., Schmaier A.A., Hynes R.O., and Kahn M.L. Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets. Blood 109 8 (2007) 3284-3290
    • (2007) Blood , vol.109 , Issue.8 , pp. 3284-3290
    • Zou, Z.1    Chen, H.2    Schmaier, A.A.3    Hynes, R.O.4    Kahn, M.L.5
  • 11
    • 4444379805 scopus 로고    scopus 로고
    • Activation of integrin alpha IIb beta 3 in the glycoprotein Ib-high population of a megakaryocytic cell line, CMK, by inside-out signaling
    • Kashiwagi H., Shiraga M., Honda S., Kosugi S., Kamae T., Kato H., Kurata Y., and Tomiyama Y. Activation of integrin alpha IIb beta 3 in the glycoprotein Ib-high population of a megakaryocytic cell line, CMK, by inside-out signaling. J. Thromb. Haemost. 2 1 (2004) 177-186
    • (2004) J. Thromb. Haemost. , vol.2 , Issue.1 , pp. 177-186
    • Kashiwagi, H.1    Shiraga, M.2    Honda, S.3    Kosugi, S.4    Kamae, T.5    Kato, H.6    Kurata, Y.7    Tomiyama, Y.8
  • 12
    • 0024509915 scopus 로고
    • A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells
    • Cheresh D.A., Smith J.W., Cooper H.M., and Quaranta V. A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells. Cell 57 1 (1989) 59-69
    • (1989) Cell , vol.57 , Issue.1 , pp. 59-69
    • Cheresh, D.A.1    Smith, J.W.2    Cooper, H.M.3    Quaranta, V.4
  • 13
    • 0028362876 scopus 로고
    • Requirement of vascular integrin alpha v beta 3 for angiogenesis
    • Brooks P.C., Clark R.A., and Cheresh D.A. Requirement of vascular integrin alpha v beta 3 for angiogenesis. Science 264 5158 (1994) 569-571
    • (1994) Science , vol.264 , Issue.5158 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 15
    • 28544452516 scopus 로고    scopus 로고
    • A direct test of potential roles for beta3 and beta5 integrins in growth and metastasis of murine mammary carcinomas
    • Taverna D., Crowley D., Connolly M., Bronson R.T., and Hynes R.O. A direct test of potential roles for beta3 and beta5 integrins in growth and metastasis of murine mammary carcinomas. Cancer Res. 65 22 (2005) 10324-10329
    • (2005) Cancer Res. , vol.65 , Issue.22 , pp. 10324-10329
    • Taverna, D.1    Crowley, D.2    Connolly, M.3    Bronson, R.T.4    Hynes, R.O.5
  • 16
    • 0030901145 scopus 로고    scopus 로고
    • Insulin-like growth factor receptor cooperates with integrin alpha v beta 5 to promote tumor cell dissemination in vivo
    • Brooks P.C., Klemke R.L., Schon S., Lewis J.M., Schwartz M.A., and Cheresh D.A. Insulin-like growth factor receptor cooperates with integrin alpha v beta 5 to promote tumor cell dissemination in vivo. J. Clin. Invest. 99 6 (1997) 1390-1398
    • (1997) J. Clin. Invest. , vol.99 , Issue.6 , pp. 1390-1398
    • Brooks, P.C.1    Klemke, R.L.2    Schon, S.3    Lewis, J.M.4    Schwartz, M.A.5    Cheresh, D.A.6
  • 17
    • 0028043735 scopus 로고
    • Receptor tyrosine kinase signaling required for integrin alpha v beta 5-directed cell motility but not adhesion on vitronectin
    • Klemke R.L., Yebra M., Bayna E.M., and Cheresh D.A. Receptor tyrosine kinase signaling required for integrin alpha v beta 5-directed cell motility but not adhesion on vitronectin. J. Cell Biol. 127 3 (1994) 859-866
    • (1994) J. Cell Biol. , vol.127 , Issue.3 , pp. 859-866
    • Klemke, R.L.1    Yebra, M.2    Bayna, E.M.3    Cheresh, D.A.4
  • 18
    • 0029759727 scopus 로고    scopus 로고
    • Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation
    • Lewis J.M., Cheresh D.A., and Schwartz M.A. Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation. J. Cell Biol. 134 5 (1996) 1323-1332
    • (1996) J. Cell Biol. , vol.134 , Issue.5 , pp. 1323-1332
    • Lewis, J.M.1    Cheresh, D.A.2    Schwartz, M.A.3
  • 19
    • 0031755756 scopus 로고    scopus 로고
    • The vitronectin receptor associates with clathrin-coated membrane domains via the cytoplasmic domain of its beta5 subunit
    • De Deyne P.G., O'Neill A., Resneck W.G., Dmytrenko G.M., Pumplin D.W., and Bloch R.J. The vitronectin receptor associates with clathrin-coated membrane domains via the cytoplasmic domain of its beta5 subunit. J. Cell Sci. 111 Pt 18 (1998) 2729-2740
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 18 , pp. 2729-2740
    • De Deyne, P.G.1    O'Neill, A.2    Resneck, W.G.3    Dmytrenko, G.M.4    Pumplin, D.W.5    Bloch, R.J.6
  • 20
    • 0027166647 scopus 로고
    • Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment
    • Wickham T.J., Mathias P., Cheresh D.A., and Nemerow G.R. Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment. Cell 73 2 (1993) 309-319
    • (1993) Cell , vol.73 , Issue.2 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 21
    • 3543053363 scopus 로고    scopus 로고
    • Immature dendritic cells phagocytose apoptotic cells via alphavbeta5 and CD36, and cross-present antigens to cytotoxic T lymphocytes
    • Albert M.L., Pearce S.F., Francisco L.M., Sauter B., Roy P., Silverstein R.L., and Bhardwaj N. Immature dendritic cells phagocytose apoptotic cells via alphavbeta5 and CD36, and cross-present antigens to cytotoxic T lymphocytes. J. Exp. Med. 188 7 (1998) 1359-1368
    • (1998) J. Exp. Med. , vol.188 , Issue.7 , pp. 1359-1368
    • Albert, M.L.1    Pearce, S.F.2    Francisco, L.M.3    Sauter, B.4    Roy, P.5    Silverstein, R.L.6    Bhardwaj, N.7
  • 22
    • 0347532862 scopus 로고    scopus 로고
    • Role of alphavbeta5 integrin in regulating phagocytosis by the retinal pigment epithelium
    • Finnemann S.C. Role of alphavbeta5 integrin in regulating phagocytosis by the retinal pigment epithelium. Adv. Exp. Med. Biol. 533 (2003) 337-342
    • (2003) Adv. Exp. Med. Biol. , vol.533 , pp. 337-342
    • Finnemann, S.C.1
  • 23
    • 0037046580 scopus 로고    scopus 로고
    • Identification of a factor that links apoptotic cells to phagocytes
    • Hanayama R., Tanaka M., Miwa K., Shinohara A., Iwamatsu A., and Nagata S. Identification of a factor that links apoptotic cells to phagocytes. Nature 417 6885 (2002) 182-187
    • (2002) Nature , vol.417 , Issue.6885 , pp. 182-187
    • Hanayama, R.1    Tanaka, M.2    Miwa, K.3    Shinohara, A.4    Iwamatsu, A.5    Nagata, S.6
  • 24
    • 0345731228 scopus 로고    scopus 로고
    • The opsonin MFG-E8 is a ligand for the alphavbeta5 integrin and triggers DOCK180-dependent Rac1 activation for the phagocytosis of apoptotic cells
    • Akakura S., Singh S., Spataro M., Akakura R., Kim J.I., Albert M.L., and Birge R.B. The opsonin MFG-E8 is a ligand for the alphavbeta5 integrin and triggers DOCK180-dependent Rac1 activation for the phagocytosis of apoptotic cells. Exp. Cell Res. 292 2 (2004) 403-416
    • (2004) Exp. Cell Res. , vol.292 , Issue.2 , pp. 403-416
    • Akakura, S.1    Singh, S.2    Spataro, M.3    Akakura, R.4    Kim, J.I.5    Albert, M.L.6    Birge, R.B.7
  • 25
    • 1542514711 scopus 로고    scopus 로고
    • Expression of developmental endothelial locus-1 in a subset of macrophages for engulfment of apoptotic cells
    • Hanayama R., Tanaka M., Miwa K., and Nagata S. Expression of developmental endothelial locus-1 in a subset of macrophages for engulfment of apoptotic cells. J. Immunol. 172 6 (2004) 3876-3882
    • (2004) J. Immunol. , vol.172 , Issue.6 , pp. 3876-3882
    • Hanayama, R.1    Tanaka, M.2    Miwa, K.3    Nagata, S.4
  • 27
    • 0033625871 scopus 로고    scopus 로고
    • αvβ5 Integrin recruits the CrkII-Dock180-rac1 complex for phagocytosis of apoptotic cells
    • Albert M.L., Kim J.I., and Birge R.B. αvβ5 Integrin recruits the CrkII-Dock180-rac1 complex for phagocytosis of apoptotic cells. Nat. Cell Biol. 2 12 (2000) 899-905
    • (2000) Nat. Cell Biol. , vol.2 , Issue.12 , pp. 899-905
    • Albert, M.L.1    Kim, J.I.2    Birge, R.B.3
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 13 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 30
    • 0026642556 scopus 로고
    • Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association
    • Reszka A.A., Hayashi Y., and Horwitz A.F. Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association. J. Cell Biol. 117 6 (1992) 1321-1330
    • (1992) J. Cell Biol. , vol.117 , Issue.6 , pp. 1321-1330
    • Reszka, A.A.1    Hayashi, Y.2    Horwitz, A.F.3
  • 31
    • 0028216712 scopus 로고
    • Identification of c-erbB-3 binding sites for phosphatidylinositol 3'-kinase and SHC using an EGF receptor/c-erbB-3 chimera
    • Prigent S.A., and Gullick W.J. Identification of c-erbB-3 binding sites for phosphatidylinositol 3'-kinase and SHC using an EGF receptor/c-erbB-3 chimera. EMBO J. 13 12 (1994) 2831-2841
    • (1994) EMBO J. , vol.13 , Issue.12 , pp. 2831-2841
    • Prigent, S.A.1    Gullick, W.J.2
  • 32
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen W.J., Goldstein J.L., and Brown M.S. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265 6 (1990) 3116-3123
    • (1990) J. Biol. Chem. , vol.265 , Issue.6 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 33
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72 (2003) 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 34
    • 0028954275 scopus 로고
    • Regulation of integrin affinity states through an NPXY motif in the beta subunit cytoplasmic domain
    • O'Toole T.E., Ylanne J., and Culley B.M. Regulation of integrin affinity states through an NPXY motif in the beta subunit cytoplasmic domain. J. Biol. Chem. 270 15 (1995) 8553-8558
    • (1995) J. Biol. Chem. , vol.270 , Issue.15 , pp. 8553-8558
    • O'Toole, T.E.1    Ylanne, J.2    Culley, B.M.3
  • 35
    • 14644411712 scopus 로고    scopus 로고
    • A role for Mer tyrosine kinase in alphavbeta5 integrin-mediated phagocytosis of apoptotic cells
    • Wu Y., Singh S., Georgescu M.M., and Birge R.B. A role for Mer tyrosine kinase in alphavbeta5 integrin-mediated phagocytosis of apoptotic cells. J. Cell Sci. 118 Pt 3 (2005) 539-553
    • (2005) J. Cell Sci. , vol.118 , Issue.PART 3 , pp. 539-553
    • Wu, Y.1    Singh, S.2    Georgescu, M.M.3    Birge, R.B.4
  • 37
    • 33645845142 scopus 로고    scopus 로고
    • Phosphatidylserine recognition by phagocytes: a view to a kill
    • Wu Y., Tibrewal N., and Birge R.B. Phosphatidylserine recognition by phagocytes: a view to a kill. Trends Cell Biol. 16 4 (2006) 189-197
    • (2006) Trends Cell Biol. , vol.16 , Issue.4 , pp. 189-197
    • Wu, Y.1    Tibrewal, N.2    Birge, R.B.3
  • 38
    • 3042609771 scopus 로고    scopus 로고
    • Talin controls integrin activation
    • Calderwood D.A. Talin controls integrin activation. Biochem. Soc. Trans. 32 Pt 3 (2004) 434-437
    • (2004) Biochem. Soc. Trans. , vol.32 , Issue.PART 3 , pp. 434-437
    • Calderwood, D.A.1
  • 40
    • 4043057284 scopus 로고    scopus 로고
    • The talin-tail interaction places integrin activation on FERM ground
    • Campbell I.D., and Ginsberg M.H. The talin-tail interaction places integrin activation on FERM ground. Trends Biochem. Sci. 29 8 (2004) 429-435
    • (2004) Trends Biochem. Sci. , vol.29 , Issue.8 , pp. 429-435
    • Campbell, I.D.1    Ginsberg, M.H.2


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