메뉴 건너뛰기




Volumn 12, Issue 12, 2007, Pages 1329-1338

Structural basis of PSGL-1 binding to ERM proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; EZRIN; HISTIDINE; METHIONINE; MOESIN; P SELECTIN GLYCOPROTEIN LIGAND 1; RADIXIN;

EID: 36849051516     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2007.01137.x     Document Type: Article
Times cited : (31)

References (43)
  • 2
    • 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.R. & Furthmayr, H. (1995) Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment and cell-cell contacts. Exp. Cell Res. 219, 180-196.
    • (1995) Exp. Cell Res. , vol.219 , pp. 180-196
    • Amieva, M.R.1    Furthmayr, H.2
  • 5
    • 17844383345 scopus 로고    scopus 로고
    • Signaling function of PSGL-1 in neutrophil: Tyrosine-phosphorylation-dependent and c-Abl-involved alteration in the F-actin-based cytoskeleton
    • Ba, X., Chen, C., Gao, Y. & Zeng, X. (2005) Signaling function of PSGL-1 in neutrophil: Tyrosine-phosphorylation-dependent and c-Abl-involved alteration in the F-actin-based cytoskeleton. J. Cell. Biochem. 94, 365-373.
    • (2005) J. Cell. Biochem. , vol.94 , pp. 365-373
    • Ba, X.1    Chen, C.2    Gao, Y.3    Zeng, X.4
  • 6
    • 0032499260 scopus 로고    scopus 로고
    • Chemokines and leukocyte traffic
    • Baggiolini, M. (1998) Chemokines and leukocyte traffic. Nature 392, 565-568.
    • (1998) Nature , vol.392 , pp. 565-568
    • Baggiolini, M.1
  • 7
    • 0028821843 scopus 로고
    • Ezrin oligomers are major cytoskeletal components of placental microvilli: A proposal for their involvement in cortical morphogenesis
    • Berryman, M., Gary, R. & Bretscher, A. (1995) Ezrin oligomers are major cytoskeletal components of placental microvilli: A proposal for their involvement in cortical morphogenesis. J. Cell Biol. 131, 1231-1242.
    • (1995) J. Cell Biol. , vol.131 , pp. 1231-1242
    • Berryman, M.1    Gary, R.2    Bretscher, A.3
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 10
    • 0028863513 scopus 로고
    • Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix: involvement of cAMP signaling pathways
    • del Pozo, M.A., Sánchez-Mateos, P., Nieto, M. & Sánchez-Madrid, F. (1995) Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix: Involvement of cAMP signaling pathways. J. Cell Biol. 131, 495-508.
    • (1995) J. Cell Biol. , vol.131 , pp. 495-508
    • del Pozo, M.A.1    Sánchez-Mateos, P.2    Nieto, M.3    Sánchez-Madrid, F.4
  • 11
    • 0037155874 scopus 로고    scopus 로고
    • Processing of integrin α v subunit by membrane type 1 matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase
    • Deryugina, E.I., Ratnikov, B.I., Postnova, T.I., Rozanov, D.V. & Strongin, A.Y. (2002) Processing of integrin α v subunit by membrane type 1 matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase. J. Biol. Chem. 277, 9749-9756.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9749-9756
    • Deryugina, E.I.1    Ratnikov, B.I.2    Postnova, T.I.3    Rozanov, D.V.4    Strongin, A.Y.5
  • 12
    • 0030064894 scopus 로고    scopus 로고
    • Chemoattractant-induced changes in surface expression and redistribution of a functional ligand for P-selectin on neutrophils
    • Doré, M., Burns, A.R., Hughes, B.J., Entman, M.L. & Smith, C.W. (1996) Chemoattractant-induced changes in surface expression and redistribution of a functional ligand for P-selectin on neutrophils. Blood 87, 2029-2037.
    • (1996) Blood , vol.87 , pp. 2029-2037
    • Doré, M.1    Burns, A.R.2    Hughes, B.J.3    Entman, M.L.4    Smith, C.W.5
  • 13
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration
    • Endo, K., Takino, T., Miyamori, H., Kinsen, H., Yoshizaki, T., Furukawa, M. & Sato, H. (2003) Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J. Biol. Chem. 278, 40764-40770.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40764-40770
    • Endo, K.1    Takino, T.2    Miyamori, H.3    Kinsen, H.4    Yoshizaki, T.5    Furukawa, M.6    Sato, H.7
  • 15
    • 33846529557 scopus 로고    scopus 로고
    • PSGL-1 and mTOR regulate translation of ROCK-1 and physiological functions of macrophages
    • Fox, R., Nhan, T.Q., Law, G.L., Morris, D.R., Liles, W.C. & Schwartz, S.M. (2007) PSGL-1 and mTOR regulate translation of ROCK-1 and physiological functions of macrophages. EMBO J. 26, 505-515.
    • (2007) EMBO J. , vol.26 , pp. 505-515
    • Fox, R.1    Nhan, T.Q.2    Law, G.L.3    Morris, D.R.4    Liles, W.C.5    Schwartz, S.M.6
  • 16
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada, K., Shimizu, T., Matsui, T., Tsukita, Sh., Tsukita, Sa. & Hakoshima, T. (2000) Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19, 4449-4462.
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, Sh.4    Tsukita, Sa.5    Hakoshima, T.6
  • 17
    • 0037415682 scopus 로고    scopus 로고
    • Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex
    • Hamada, K., Shimizu, T., Yonemura, S., Tsukita, Sh., Tsukita, Sa. & Hakoshima, T. (2003) Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex. EMBO J. 22, 502-514.
    • (2003) EMBO J. , vol.22 , pp. 502-514
    • Hamada, K.1    Shimizu, T.2    Yonemura, S.3    Tsukita, S.h.4    Tsukita, S.a.5    Hakoshima, T.6
  • 18
    • 0030661712 scopus 로고    scopus 로고
    • Engagement of P-selectin glycoprotein ligand-1 enhances tyrosine phosphorylation and activates mitogen-activated protein kinases in human neutrophils
    • Hidari, K.I., Weyrich, A.S., Zimmerman, G.A. & McEver, R.P. (1997) Engagement of P-selectin glycoprotein ligand-1 enhances tyrosine phosphorylation and activates mitogen-activated protein kinases in human neutrophils. J. Biol. Chem. 272, 28750-28756.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28750-28756
    • Hidari, K.I.1    Weyrich, A.S.2    Zimmerman, G.A.3    McEver, R.P.4
  • 19
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: A potent modifier of pericellular microenvironment
    • Itoh, Y. & Seiki, M. (2006) MT1-MMP: A potent modifier of pericellular microenvironment. J. Cell. Physiol. 206, 1-8.
    • (2006) J. Cell. Physiol. , vol.206 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita, M., Itoh, Y., Chiba, T., Mori, H., Okada, A., Kinoh, H. & Seiki, M. (2001). Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J. Cell Biol. 153, 893-904.
    • (2001) J. Cell Biol. , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 22
    • 0029858031 scopus 로고    scopus 로고
    • Selectins and their ligands: Current concepts and controversies
    • Kansas, G.S. (1996) Selectins and their ligands: Current concepts and controversies. Blood 88, 3259-3287.
    • (1996) Blood , vol.88 , pp. 3259-3287
    • Kansas, G.S.1
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 0032509889 scopus 로고    scopus 로고
    • Chemokines-chemotactic cytokines that mediate inflammation
    • Luster, A.D. (1998) Chemokines-chemotactic cytokines that mediate inflammation. N Engl. J. Med. 338, 436-445.
    • (1998) N Engl. J. Med. , vol.338 , pp. 436-445
    • Luster, A.D.1
  • 26
    • 0032940071 scopus 로고    scopus 로고
    • ERM proteins in cell adhesion and membrane dynamics
    • Mangeat, P., Roy, C. & Martin, M. (1999) ERM proteins in cell adhesion and membrane dynamics. Trends Cell Biol. 9, 187-192.
    • (1999) Trends Cell Biol. , vol.9 , pp. 187-192
    • Mangeat, P.1    Roy, C.2    Martin, M.3
  • 27
    • 0030854107 scopus 로고    scopus 로고
    • Perspectives series: Cell adhesion in vascular biology. Role of PSGL-1 binding to selectins in leukocyte recruitment
    • McEver, R.P. & Cummings, R.D. (1997) Perspectives series: Cell adhesion in vascular biology. Role of PSGL-1 binding to selectins in leukocyte recruitment. J Clin. Invest. 100, 485-491.
    • (1997) J Clin. Invest. , vol.100 , pp. 485-491
    • McEver, R.P.1    Cummings, R.D.2
  • 28
    • 0014686253 scopus 로고
    • Microspikes on the lymphocyte uropod
    • McFarland, W. (1969) Microspikes on the lymphocyte uropod. Science 163, 818-820.
    • (1969) Science , vol.163 , pp. 818-820
    • McFarland, W.1
  • 32
    • 0029116771 scopus 로고
    • Differential expression of the microspike-associate protein moesin in human tissues
    • Schwartz-Albiez, R., Merling, A., Spring, H., Möller, P. & Korenz, K. (1995) Differential expression of the microspike-associate protein moesin in human tissues. Eur. J. Cell Biol. 67, 189-198.
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 189-198
    • Schwartz-Albiez, R.1    Merling, A.2    Spring, H.3    Möller, P.4    Korenz, K.5
  • 33
    • 0036080407 scopus 로고    scopus 로고
    • A juxta-membrane amino acid sequence of P-selectin glycoprotein ligand-1 is involved in moesin binding and ezrin/radixin/moesin-directed targeting at the trailing edge of migrating lymphocytes
    • Serrador, J.M., Urzainqui, A., Alonso-Lebrero, J.L., Cabrero, J.R., Montoya, M.C., Vicente-Manzanares, M., Yáñez-Mó, M. & Sánchez-Madrid, F. (2002) A juxta-membrane amino acid sequence of P-selectin glycoprotein ligand-1 is involved in moesin binding and ezrin/radixin/moesin-directed targeting at the trailing edge of migrating lymphocytes. Eur. J. Immunol. 32, 1560-1566.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1560-1566
    • Serrador, J.M.1    Urzainqui, A.2    Alonso-Lebrero, J.L.3    Cabrero, J.R.4    Montoya, M.C.5    Vicente-Manzanares, M.6    Yanez-Mo, M.7    Sanchez-Madrid, F.8
  • 34
    • 0022270544 scopus 로고
    • Behaviour of neutrophil leukocytes in uniform concentrations of chemotactic factors: Contraction waves, cell polarity and persistence
    • Shields, J.M. & Haston, W.S. (1985) Behaviour of neutrophil leukocytes in uniform concentrations of chemotactic factors: Contraction waves, cell polarity and persistence. J. Cell Sci. 74, 75-93.
    • (1985) J. Cell Sci. , vol.74 , pp. 75-93
    • Shields, J.M.1    Haston, W.S.2
  • 35
    • 0037097835 scopus 로고    scopus 로고
    • Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin
    • Snapp, K.R., Heitzig, C.E. & Kansas, G.S. (2002) Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin. Blood 99, 4494-4502.
    • (2002) Blood , vol.99 , pp. 4494-4502
    • Snapp, K.R.1    Heitzig, C.E.2    Kansas, G.S.3
  • 36
    • 33846042975 scopus 로고    scopus 로고
    • Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1
    • Takai, Y., Kitano, K., Terawaki, S., Maesaki R. & Hakoshima T. (2007) Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1. Acta Crystallogr. F 63, 49-51.
    • (2007) Acta Crystallogr. F , vol.63 , pp. 49-51
    • Takai, Y.1    Kitano, K.2    Terawaki, S.3    Maesaki, R.4    Hakoshima, T.5
  • 37
    • 33645992471 scopus 로고    scopus 로고
    • Structural basis for NHERF recognition by ERM proteins
    • Terawaki, S., Maesaki, R. & Hakoshima, T. (2006) Structural basis for NHERF recognition by ERM proteins. Structure 14, 777-789.
    • (2006) Structure , vol.14 , pp. 777-789
    • Terawaki, S.1    Maesaki, R.2    Hakoshima, T.3
  • 38
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: Lessons from ERM (ezrin/radixin/moesin) proteins
    • Tsukita, Sa. & Yonemura, S. (1999) Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J. Biol. Chem. 274, 34507-34510.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34507-34510
    • Tsukita, Sa.1    Yonemura, S.2
  • 39
    • 0031043523 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin) family: From cytoskeleton to signal transduction
    • Tsukita, Sa., Yonemura, S. & Tsukita, Sh. (1997) ERM (ezrin/radixin/ moesin) family: From cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9, 70-75.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 70-75
    • Tsukita, Sa.1    Yonemura, S.2    Tsukita, Sh.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.