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Volumn 14, Issue 4, 2003, Pages 211-217

Platelet moesin interacts with PECAM-1 (CD31)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CD31 ANTIGEN; EZRIN; MOESIN; RADIXIN; THROMBIN;

EID: 0037711542     PISSN: 09537104     EISSN: None     Source Type: Journal    
DOI: 10.1080/0953710031000118830     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 0026784141 scopus 로고
    • Mechanisms of actin rearrangements mediating platelet activation
    • Hartwig J H. Mechanisms of actin rearrangements mediating platelet activation. J Cell Biol 1992; 118: 1421-42.
    • (1992) J Cell Biol , vol.118 , pp. 1421-1442
    • Hartwig, J.H.1
  • 2
    • 0027748236 scopus 로고
    • The platelet cytoskeleton
    • Fox J E B. The platelet cytoskeleton. Thromb Haemost 1993; 70: 884-93.
    • (1993) Thromb Haemost , vol.70 , pp. 884-893
    • Fox, J.E.B.1
  • 3
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membranes association sites
    • Sato N, Funayama N, Nagabuchi A, Yonemura S, Tsukita S, Tsukita S. A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membranes association sites. J Cell Sci 1992; 103: 131-43.
    • (1992) J Cell Sci , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagabuchi, A.3    Yonemura, S.4    Tsukita, S.5    Tsukita, S.6
  • 5
    • 0029086637 scopus 로고
    • Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts
    • Amieva M A, Furthmayr H. Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. Exp Cell Res 1995; 219: 180-96.
    • (1995) Exp Cell Res , vol.219 , pp. 180-196
    • Amieva, M.A.1    Furthmayr, H.2
  • 7
    • 0029116771 scopus 로고
    • Differential expression of the microspikes-associated protein moesin in human tissues
    • Schwartz-Albiez R, Merling A, Spring H, Moller P, Koretz K. Differential expression of the microspikes-associated protein moesin in human tissues. Eur J Cell Biol 1995; 67: 189-98.
    • (1995) Eur J Cell Biol , vol.67 , pp. 189-198
    • Schwartz-Albiez, R.1    Merling, A.2    Spring, H.3    Moller, P.4    Koretz, K.5
  • 8
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
    • Bretscher A, Reczek D, Berryman M. Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J Cell Sci 1997; 110: 3011-8.
    • (1997) J Cell Sci , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 9
    • 0031240066 scopus 로고    scopus 로고
    • Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts
    • Lamb R F, Ozanne B W, Roy C, McGarry L, Stipp C, Mangeat P, Jay D G. Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts. Curr Biol 1997; 7: 682-8.
    • (1997) Curr Biol , vol.7 , pp. 682-688
    • Lamb, R.F.1    Ozanne, B.W.2    Roy, C.3    McGarry, L.4    Stipp, C.5    Mangeat, P.6    Jay, D.G.7
  • 10
    • 0028229539 scopus 로고
    • ERM family members as linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita S, Oishi K, Sato N, Sagara J, Kawai A, Tsukita S. ERM family members as linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol 1994; 126: 391-401.
    • (1994) J Cell Biol , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 11
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita S, Tsukita S. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol 1996; 135: 37-51.
    • (1996) J Cell Biol , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 12
    • 0030847406 scopus 로고    scopus 로고
    • Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarisation
    • Serrador J M, Alonso-Lebrero J L, del Pozo M A, Furthmayr H, Schwartz-Albiez R, Calvo J, Lonzano F, Sanchez-Madrid F. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarisation. J Cell Biol 1997; 138: 1409-26.
    • (1997) J Cell Biol , vol.138 , pp. 1409-1426
    • Serrador, J.M.1    Alonso-Lebrero, J.L.2    Del Pozo, M.A.3    Furthmayr, H.4    Schwartz-Albiez, R.5    Calvo, J.6    Lonzano, F.7    Sanchez-Madrid, F.8
  • 14
    • 0032482323 scopus 로고    scopus 로고
    • Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44
    • Legg J W, Isacke C M. Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44. Curr Biol 1998; 8: 705-8.
    • (1998) Curr Biol , vol.8 , pp. 705-708
    • Legg, J.W.1    Isacke, C.M.2
  • 15
    • 0032555599 scopus 로고    scopus 로고
    • Association of ezrin with intercellular molecule-1 and -2 (ICAM-1 and ICAM-2)
    • Heiska L, Alfthan K, Grönholm M, Vilja P, Vaheri A, Carpén O. Association of ezrin with intercellular molecule-1 and -2 (ICAM-1 and ICAM-2). J Biol Chem 1998; 273: 21893-900.
    • (1998) J Biol Chem , vol.273 , pp. 21893-21900
    • Heiska, L.1    Alfthan, K.2    Grönholm, M.3    Vilja, P.4    Vaheri, A.5    Carpén, O.6
  • 16
    • 0033612533 scopus 로고    scopus 로고
    • Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins
    • Yonemura S, Tsukita S, Tsukita S. Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J Cell Biol 1999; 145: 1497-509.
    • (1999) J Cell Biol , vol.145 , pp. 1497-1509
    • Yonemura, S.1    Tsukita, S.2    Tsukita, S.3
  • 17
    • 0032940071 scopus 로고    scopus 로고
    • ERM proteins in cell adhesion and membrane dynamics
    • Mangeat P, Roy C, Martin M. ERM proteins in cell adhesion and membrane dynamics. Trends Cell Biol 1999; 9: 187-92.
    • (1999) Trends Cell Biol , vol.9 , pp. 187-192
    • Mangeat, P.1    Roy, C.2    Martin, M.3
  • 18
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: Lessons from ERM (ezrin/radixin/moesin) proteins
    • Tsukita S, Yonemura S. Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J Biol Chem 1999; 274: 34507-10.
    • (1999) J Biol Chem , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 19
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    • Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita S, Tsukita S. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol 1998; 140: 647-57.
    • (1998) J Cell Biol , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, S.7    Tsukita, S.8
  • 20
    • 0034631843 scopus 로고    scopus 로고
    • Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane
    • Gautreau A, Louvard D, Arpin M. Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane. J Cell Biol 2000; 150: 193-203.
    • (2000) J Cell Biol , vol.150 , pp. 193-203
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 21
    • 0026091353 scopus 로고
    • Moesin: A member of the protein 4.1-talin-ezrin family of proteins
    • Lankes W T, Furthmayr H. Moesin: a member of the protein 4.1-talin-ezrin family of proteins. Proc Natl Acad Sci USA 1991; 88: 8297-301.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8297-8301
    • Lankes, W.T.1    Furthmayr, H.2
  • 22
    • 0029569120 scopus 로고
    • Phosphorylation of threonine 558 in the carboxyl-terminal actin binding domain of moesin by thrombin activation of human platelets
    • Nakamura F, Amieva M R, Furthmayr H. Phosphorylation of threonine 558 in the carboxyl-terminal actin binding domain of moesin by thrombin activation of human platelets. J Biol Chem 1995; 270: 31377-85.
    • (1995) J Biol Chem , vol.270 , pp. 31377-31385
    • Nakamura, F.1    Amieva, M.R.2    Furthmayr, H.3
  • 23
    • 0032783917 scopus 로고    scopus 로고
    • Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphoinositides
    • Nakamura F, Huang L, Pestonjamasp K, Luna E, Furthmayr H. Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphoinositides. Mol Biol Cell 1999; 10: 2669-85.
    • (1999) Mol Biol Cell , vol.10 , pp. 2669-2685
    • Nakamura, F.1    Huang, L.2    Pestonjamasp, K.3    Luna, E.4    Furthmayr, H.5
  • 24
    • 0033560029 scopus 로고    scopus 로고
    • Dynamic association of moesin with membrane cytoskeleton of thrombin-activated platelets
    • Shcherbina A, Kenney D M, Bretscher A, Remold-O'Donnell E. Dynamic association of moesin with membrane cytoskeleton of thrombin-activated platelets. Blood 1999; 93: 2128-9.
    • (1999) Blood , vol.93 , pp. 2128-2129
    • Shcherbina, A.1    Kenney, D.M.2    Bretscher, A.3    Remold-O'Donnell, E.4
  • 25
    • 0025274020 scopus 로고
    • PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily
    • Newman P J, Berndt M C, Gorski J, White G C, Lyman S, Paddock C, Muller W A. PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily. Science 1990; 247: 1219-22.
    • (1990) Science , vol.247 , pp. 1219-1222
    • Newman, P.J.1    Berndt, M.C.2    Gorski, J.3    White, G.C.4    Lyman, S.5    Paddock, C.6    Muller, W.A.7
  • 26
    • 0025873304 scopus 로고
    • Molecular and cellular properties of PECAM-1 (endoCAM/CD31): A novel vascular cell-cell adhesion molecule
    • Albelda S, Muller W, Buck C, Newman P. Molecular and cellular properties of PECAM-I (endoCAM/CD31): a novel vascular cell-cell adhesion molecule. J Cell Biol 1991; 114: 1059-68.
    • (1991) J Cell Biol , vol.114 , pp. 1059-1068
    • Albelda, S.1    Muller, W.2    Buck, C.3    Newman, P.4
  • 27
    • 0031025201 scopus 로고    scopus 로고
    • The biology of PECAM-1
    • Newman P J. The biology of PECAM-1. J Clin Invest 1997; 99: 3-8.
    • (1997) J Clin Invest , vol.99 , pp. 3-8
    • Newman, P.J.1
  • 29
    • 0031982997 scopus 로고    scopus 로고
    • Platelet/endothelial cell adhesion molecule-1 serves as a costimulatory agonist receptor that modulates integrin-dependent adhesion and aggregation of human platelets
    • Varon D, Jackson D E, Shenkman B, Dardik R, Tamarin I, Savion N, Newman P J. Platelet/endothelial cell adhesion molecule-1 serves as a costimulatory agonist receptor that modulates integrin-dependent adhesion and aggregation of human platelets. Blood 1998; 91: 500-7.
    • (1998) Blood , vol.91 , pp. 500-507
    • Varon, D.1    Jackson, D.E.2    Shenkman, B.3    Dardik, R.4    Tamarin, I.5    Savion, N.6    Newman, P.J.7
  • 30
    • 0035825176 scopus 로고    scopus 로고
    • Integrin activation by regulated dimerization and oligomerization of platelet endothelial cell adhesion molecule (PECAM)-1 from within the cell
    • Zhao T, Newman P J. Integrin activation by regulated dimerization and oligomerization of platelet endothelial cell adhesion molecule (PECAM)-1 from within the cell. J Cell Biol 2001; 152: 65-73.
    • (2001) J Cell Biol , vol.152 , pp. 65-73
    • Zhao, T.1    Newman, P.J.2
  • 31
    • 0026779479 scopus 로고
    • Activation-dependent changes in human platelet PECAM-1: Phosphorylation, cytoskeletal association, and surface membrane distribution
    • Newman P, Hillery C, Albrecht R, Parise L, Berndt M, Mazurov A, Dunlop L, Zhang J, Rittenhouse S. Activation-dependent changes in human platelet PECAM-1: phosphorylation, cytoskeletal association, and surface membrane distribution. J Cell Biol 1992; 119: 239-46.
    • (1992) J Cell Biol , vol.119 , pp. 239-246
    • Newman, P.1    Hillery, C.2    Albrecht, R.3    Parise, L.4    Berndt, M.5    Mazurov, A.6    Dunlop, L.7    Zhang, J.8    Rittenhouse, S.9
  • 32
    • 0030936012 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase SHP-2 binds PECAM-1 and forms a distinct signaling complex during platelet aggregation: Evidence for a mechanistic link between PECAM-1 and integrin-mediated cellular signaling
    • Jackson D, Ward C, Wang R, Newman P. The protein tyrosine phosphatase SHP-2 binds PECAM-1 and forms a distinct signaling complex during platelet aggregation: evidence for a mechanistic link between PECAM-1 and integrin-mediated cellular signaling. J Biol Chem 1997; 272: 6986-93.
    • (1997) J Biol Chem , vol.272 , pp. 6986-6993
    • Jackson, D.1    Ward, C.2    Wang, R.3    Newman, P.4
  • 33
    • 0030855963 scopus 로고    scopus 로고
    • Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2
    • Jackson D, Kupcho K, Newman P. Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2. J Biol Chem 1997; 272: 24868-75.
    • (1997) J Biol Chem , vol.272 , pp. 24868-24875
    • Jackson, D.1    Kupcho, K.2    Newman, P.3
  • 34
    • 0032561357 scopus 로고    scopus 로고
    • Recruitment and activation of SHP-1 protein tyrosine phosphatase by human platelet endothelial cell adhesion molecule-1 PECAM-1
    • Hua C, Gamble J, Vadas M, Jackson D. Recruitment and activation of SHP-1 protein tyrosine phosphatase by human platelet endothelial cell adhesion molecule-1 PECAM-1. J Biol Chem 1998; 273: 28332-40.
    • (1998) J Biol Chem , vol.273 , pp. 28332-28340
    • Hua, C.1    Gamble, J.2    Vadas, M.3    Jackson, D.4
  • 35
    • 0034282684 scopus 로고    scopus 로고
    • Collagen, convulxin, and thrombin stimulate aggregation-independent tyrosine phosphorylation of CD31 in platelets
    • Cicmil M, Thomas J M, Sage T, Barry F A, Leduc M, Bon C, Gibbins J M. Collagen, convulxin, and thrombin stimulate aggregation-independent tyrosine phosphorylation of CD31 in platelets. J Biol Chem 2000; 275: 27339-47.
    • (2000) J Biol Chem , vol.275 , pp. 27339-27347
    • Cicmil, M.1    Thomas, J.M.2    Sage, T.3    Barry, F.A.4    Leduc, M.5    Bon, C.6    Gibbins, J.M.7
  • 36
    • 0020804117 scopus 로고
    • Purification of an 80,000-dalton protein that is a component of the isolated microvillous cytoskeleton, and its localization in non-muscle cells
    • Bretscher A. Purification of an 80,000-dalton protein that is a component of the isolated microvillous cytoskeleton, and its localization in non-muscle cells. J Cell Biol 1983; 97: 425-32.
    • (1983) J Cell Biol , vol.97 , pp. 425-432
    • Bretscher, A.1
  • 39
    • 0029914934 scopus 로고    scopus 로고
    • Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c-Src in human platelets
    • Falet H, Ramos-Morales F, Bachelot C, Fischer S, Rendu F. Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c-Src in human platelets. FEBS Lett 1996; 383: 165-9.
    • (1996) FEBS Lett , vol.383 , pp. 165-169
    • Falet, H.1    Ramos-Morales, F.2    Bachelot, C.3    Fischer, S.4    Rendu, F.5
  • 40
    • 0035869434 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule-1 serves as an inhibitory receptor that modulates platelet responses to collagen
    • Patil S, Newman D K, Newman P J. Platelet endothelial cell adhesion molecule-1 serves as an inhibitory receptor that modulates platelet responses to collagen. Blood 2001; 97: 1727-32.
    • (2001) Blood , vol.97 , pp. 1727-1732
    • Patil, S.1    Newman, D.K.2    Newman, P.J.3
  • 41
    • 0035469892 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecules-1 is a negative regulator of platelet-collagen interactions
    • Jones K L, Hughan S C, Dopheide S M, Farndale R W, Jackson S P, Jackson D E. Platelet endothelial cell adhesion molecules-1 is a negative regulator of platelet-collagen interactions. Blood 2001; 98: 1456-63.
    • (2001) Blood , vol.98 , pp. 1456-1463
    • Jones, K.L.1    Hughan, S.C.2    Dopheide, S.M.3    Farndale, R.W.4    Jackson, S.P.5    Jackson, D.E.6
  • 42
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig J H, Bokoch G M, Carpenter C L, Janmey P A, Taylor L A, Toker A, Stossel T P. Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 1995; 82: 643-53.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 43
    • 0030872949 scopus 로고    scopus 로고
    • Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay D J, Esch F, Furthmayr H, Hall A. Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J Cell Biol 1997; 138: 927-47.
    • (1997) J Cell Biol , vol.138 , pp. 927-947
    • Mackay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.