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Volumn 425, Issue 18, 2013, Pages 3549-3562

FERM domain of moesin desorbs the basic-rich cytoplasmic domain of L-selectin from the anionic membrane surface

Author keywords

Ectodomain shedding; Juxtamembrane region; L selectin; Moesin; Protein lipid interaction

Indexed keywords

CALMODULIN; FLUORESCENT DYE; L SELECTIN; LIPOSOME; MOESIN; NITROXIDE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE;

EID: 84883287668     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.06.008     Document Type: Article
Times cited : (11)

References (59)
  • 1
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • Arribas J, Borroto A. Protein ectodomain shedding. Chem Rev 2002;102:4627-38.
    • (2002) Chem Rev , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 2
    • 84866487100 scopus 로고    scopus 로고
    • Ectodomain shedding and ADAMs in development
    • Weber S, Saftig P. Ectodomain shedding and ADAMs in development. Development 2012;139:3693-709.
    • (2012) Development , vol.139 , pp. 3693-3709
    • Weber, S.1    Saftig, P.2
  • 4
    • 79960102280 scopus 로고    scopus 로고
    • Ectodomain shedding and remnant peptide signalling of EGFRs and their ligands
    • Higashiyama S, Nanba D, Nakayama H, Inoue H, Fukuda S. Ectodomain shedding and remnant peptide signalling of EGFRs and their ligands. J Biochem 2011;150:15-22.
    • (2011) J Biochem , vol.150 , pp. 15-22
    • Higashiyama, S.1    Nanba, D.2    Nakayama, H.3    Inoue, H.4    Fukuda, S.5
  • 6
    • 0032549712 scopus 로고    scopus 로고
    • Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism
    • Kahn J, Walcheck B, Migaki GI, Jutila MA, Kishimoto TK. Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell 1998;92:809-18.
    • (1998) Cell , vol.92 , pp. 809-818
    • Kahn, J.1    Walcheck, B.2    Migaki, G.I.3    Jutila, M.A.4    Kishimoto, T.K.5
  • 7
    • 1942542931 scopus 로고    scopus 로고
    • Ligands for L-selectin: Homing, inflammation, and beyond
    • Rosen SD. Ligands for L-selectin: homing, inflammation, and beyond. Annu Rev Immunol 2004;22:129-56.
    • (2004) Annu Rev Immunol , vol.22 , pp. 129-156
    • Rosen, S.D.1
  • 8
    • 0037127291 scopus 로고    scopus 로고
    • The cytoplasmic tail of L-selectin interacts with members of the Ezrin-Radixin-Moesin (ERM) family of proteins: Cell activation-dependent binding of Moesin but not Ezrin
    • Ivetic A, Deka J, Ridley A, Ager A. The cytoplasmic tail of L-selectin interacts with members of the Ezrin-Radixin-Moesin (ERM) family of proteins: cell activation-dependent binding of Moesin but not Ezrin. J Biol Chem 2002;277:2321-9.
    • (2002) J Biol Chem , vol.277 , pp. 2321-2329
    • Ivetic, A.1    Deka, J.2    Ridley, A.3    Ager, A.4
  • 9
    • 33749328254 scopus 로고    scopus 로고
    • ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding
    • Li Y, Brazzell J, Herrera A, Walcheck B. ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding. Blood 2006;108:2275-9.
    • (2006) Blood , vol.108 , pp. 2275-2279
    • Li, Y.1    Brazzell, J.2    Herrera, A.3    Walcheck, B.4
  • 10
    • 77952574514 scopus 로고    scopus 로고
    • The cytoplasmic domains of TNFa- converting enzyme (TACE/ADAM17) and L-selectin are regulated differently by p38 MAPK and PKC to promote ectodomain shedding
    • Killock DJ, Ivetic A. The cytoplasmic domains of TNFa- converting enzyme (TACE/ADAM17) and L-selectin are regulated differently by p38 MAPK and PKC to promote ectodomain shedding. Biochem J 2010;428: 293-304.
    • (2010) Biochem J , vol.428 , pp. 293-304
    • Killock, D.J.1    Ivetic, A.2
  • 11
    • 0028269635 scopus 로고
    • Membrane proximal cleavage of L-selectin: Identification of the cleavage site and a 6-kD transmembrane peptide fragment of L-selectin
    • Kahn J, Ingraham RH, Shirley F, Migaki GI, Kishimoto TK. Membrane proximal cleavage of L-selectin: identification of the cleavage site and a 6-kD transmembrane peptide fragment of L-selectin. J Cell Biol 1994;125:461-70.
    • (1994) J Cell Biol , vol.125 , pp. 461-470
    • Kahn, J.1    Ingraham, R.H.2    Shirley, F.3    Migaki, G.I.4    Kishimoto, T.K.5
  • 12
    • 0035425359 scopus 로고    scopus 로고
    • The cytoplasmic domain of L-selectin participates in regulating L-selectin endoproteolysis
    • Matala E, Alexander SR, Kishimoto TK, Walcheck B. The cytoplasmic domain of L-selectin participates in regulating L-selectin endoproteolysis. J Immunol 2001;167:1617-23.
    • (2001) J Immunol , vol.167 , pp. 1617-1623
    • Matala, E.1    Alexander, S.R.2    Kishimoto, T.K.3    Walcheck, B.4
  • 13
    • 4043079958 scopus 로고    scopus 로고
    • Mutagenesis of the ezrin-radixin-moesin binding domain of L-selectin tail affects shedding, microvillar positioning, and leukocyte tethering
    • Ivetic A, Florey O, Deka J, Haskard DO, Ager A, Ridley AJ. Mutagenesis of the ezrin-radixin-moesin binding domain of L-selectin tail affects shedding, microvillar positioning, and leukocyte tethering. J Biol Chem 2004;279:33263-72.
    • (2004) J Biol Chem , vol.279 , pp. 33263-33272
    • Ivetic, A.1    Florey, O.2    Deka, J.3    Haskard, D.O.4    Ager, A.5    Ridley, A.J.6
  • 14
    • 0035903233 scopus 로고    scopus 로고
    • Regulation of membrane metalloproteolytic cleavage of L-selectin (CD62L) by the epidermal growth factor domain
    • Zhao L, Shey M, Farnsworth M, Dailey MO. Regulation of membrane metalloproteolytic cleavage of L-selectin (CD62L) by the epidermal growth factor domain. J Biol Chem 2001; 276:30631-40.
    • (2001) J Biol Chem , vol.276 , pp. 30631-30640
    • Zhao, L.1    Shey, M.2    Farnsworth, M.3    Dailey, M.O.4
  • 15
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixin-moesin protein family
    • Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr Opin Cell Biol 1999;11:109-16.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 16
    • 0034524664 scopus 로고    scopus 로고
    • ERM-Merlin and EBP50 protein families in plasma membrane organization and function
    • Bretscher A, Chambers D, Nguyen R, Reczek D. ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu Rev Cell Dev Biol 2000;16:113-43.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 113-143
    • Bretscher, A.1    Chambers, D.2    Nguyen, R.3    Reczek, D.4
  • 17
    • 0026091353 scopus 로고
    • Moesin: A member of the protein 4.1-talin-ezrin family of proteins
    • Lankes WT, 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
  • 18
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 2000;101:259-70.
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 19
    • 0033617289 scopus 로고    scopus 로고
    • Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin. Regulation by conformational change
    • Huang L, Wong TY, Lin RC, Furthmayr H. Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin. Regulation by conformational change. J Biol Chem 1999; 274:12803-10.
    • (1999) J Biol Chem , vol.274 , pp. 12803-12810
    • Huang, L.1    Wong, T.Y.2    Lin, R.C.3    Furthmayr, H.4
  • 20
    • 0032783917 scopus 로고    scopus 로고
    • Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides
    • Nakamura F, Huang L, Pestonjamasp K, Luna EJ, Furthmayr H. Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides. 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.J.4    Furthmayr, H.5
  • 21
    • 0035912664 scopus 로고    scopus 로고
    • The 2.7 Å crystal structure of the activated FERM domain of moesin: An analysis of structural changes on activation
    • Edwards SD, Keep NH. The 2.7 Å crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation. Biochemistry 2001;40:7061-8.
    • (2001) Biochemistry , vol.40 , pp. 7061-7068
    • Edwards, S.D.1    Keep, N.H.2
  • 22
    • 84868262769 scopus 로고    scopus 로고
    • Open conformation of ezrin bound to phosphatidylinositol 4, 5-bisphosphate and to F-actin revealed by neutron scattering
    • Jayasundar JJ, Ju JH, He L, Liu D, Meilleur F, Zhao J, et al. Open conformation of ezrin bound to phosphatidylinositol 4, 5-bisphosphate and to F-actin revealed by neutron scattering. J Biol Chem 2012;287:37119-33.
    • (2012) J Biol Chem , vol.287 , pp. 37119-37133
    • Jayasundar, J.J.1    Ju, J.H.2    He, L.3    Liu, D.4    Meilleur, F.5    Zhao, J.6
  • 23
    • 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 polarization
    • Serrador JM, Alonso-Lebrero JL, del Pozo MA, Furthmayr H, Schwartz-Albiez R, Calvo J, et al. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization. J Cell Biol 1997;138:1409-23.
    • (1997) J Cell Biol , vol.138 , pp. 1409-1423
    • Serrador, J.M.1    Alonso-Lebrero, J.L.2    Del Pozo, M.A.3    Furthmayr, H.4    Schwartz-Albiez, R.5    Calvo, J.6
  • 24
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J Cell Biol 1998;140:885-95.
    • (1998) J Cell Biol , vol.140 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6
  • 25
    • 58549102340 scopus 로고    scopus 로고
    • The protein kinase A-anchoring protein moesin is bound to pigment granules in melanophores
    • Semenova I, Ikeda K, Ivanov P, Rodionov V. The protein kinase A-anchoring protein moesin is bound to pigment granules in melanophores. Traffic 2009;10:153-60.
    • (2009) Traffic , vol.10 , pp. 153-160
    • Semenova, I.1    Ikeda, K.2    Ivanov, P.3    Rodionov, V.4
  • 27
    • 0037166942 scopus 로고    scopus 로고
    • Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes
    • Barreiro O, Yanez-Mo M, Serrador JM, Montoya MC, Vicente-Manzanares M, Tejedor R, et al. Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J Cell Biol 2002;157:1233-45.
    • (2002) J Cell Biol , vol.157 , pp. 1233-1245
    • Barreiro, O.1    Yanez-Mo, M.2    Serrador, J.M.3    Montoya, M.C.4    Vicente-Manzanares, M.5    Tejedor, R.6
  • 28
    • 10644290857 scopus 로고    scopus 로고
    • The telling tail of L-selectin
    • Ivetic A, Ridley AJ. The telling tail of L-selectin. Biochem Soc Trans 2004;32:1118-21.
    • (2004) Biochem Soc Trans , vol.32 , pp. 1118-1121
    • Ivetic, A.1    Ridley, A.J.2
  • 29
    • 79960697734 scopus 로고    scopus 로고
    • Interaction of calmodulin with L-selectin at the membrane interface: Implication on the regulation of L-selectin shedding
    • Deng W, Srinivasan S, Zheng X, Putkey JA, Li R. Interaction of calmodulin with L-selectin at the membrane interface: implication on the regulation of L-selectin shedding. J Mol Biol 2011;411:220-33.
    • (2011) J Mol Biol , vol.411 , pp. 220-233
    • Deng, W.1    Srinivasan, S.2    Zheng, X.3    Putkey, J.A.4    Li, R.5
  • 30
    • 65649085856 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of molecular interactions between calmodulin, Ezrin/Radixin/- Moesin, and L-selectin
    • Killock DJ, Parsons M, Zarrouk M, Ameer-Beg SM, Ridley AJ, Haskard DO, et al. In vitro and in vivo characterization of molecular interactions between calmodulin, Ezrin/Radixin/- Moesin, and L-selectin. J Biol Chem 2009;284:8833-45.
    • (2009) J Biol Chem , vol.284 , pp. 8833-8845
    • Killock, D.J.1    Parsons, M.2    Zarrouk, M.3    Ameer-Beg, S.M.4    Ridley, A.J.5    Haskard, D.O.6
  • 31
    • 79954878303 scopus 로고    scopus 로고
    • L-selectin transmembrane and cytoplasmic domains are monomeric in membranes
    • Srinivasan S, Deng W, Li R. L-Selectin transmembrane and cytoplasmic domains are monomeric in membranes. Biochim Biophys Acta 2011;1808:1709-15.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1709-1715
    • Srinivasan, S.1    Deng, W.2    Li, R.3
  • 32
    • 84864465448 scopus 로고    scopus 로고
    • Binding of moesin and ezrin to membranes containing phosphatidylinositol (4,5) bisphosphate a comparative study of the affinity constants and conformational changes
    • Maniti O, Khalifat N, Goggia K, Dalonneau F, Guerin C, Blanchoin L, et al. Binding of moesin and ezrin to membranes containing phosphatidylinositol (4, 5) bisphosphate: a comparative study of the affinity constants and conformational changes. Biochim Biophys Acta 2012;1818:2839-49.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 2839-2849
    • Maniti, O.1    Khalifat, N.2    Goggia, K.3    Dalonneau, F.4    Guerin, C.5    Blanchoin, L.6
  • 33
    • 38549106998 scopus 로고    scopus 로고
    • Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol 4, 5 bisphosphate
    • Blin G, Margeat E, Carvalho K, Royer CA, Roy C, Picart C. Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol 4, 5 bisphosphate. Biophys J 2008;94:1021-33.
    • (2008) Biophys J , vol.94 , pp. 1021-1033
    • Blin, G.1    Margeat, E.2    Carvalho, K.3    Royer, C.A.4    Roy, C.5    Picart, C.6
  • 34
    • 0029900789 scopus 로고    scopus 로고
    • Conformational transitions monitored for single molecules in solution
    • Edman L, Mets U, Rigler R. Conformational transitions monitored for single molecules in solution. Proc Natl Acad Sci USA 1996;93:6710-5.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6710-6715
    • Edman, L.1    Mets, U.2    Rigler, R.3
  • 35
    • 0032539686 scopus 로고    scopus 로고
    • Monitoring conformational dynamics of a single molecule by selective fluorescence spectroscopy
    • Eggeling C, Fries JR, Brand L, Gunther R, Seidel CA. Monitoring conformational dynamics of a single molecule by selective fluorescence spectroscopy. Proc Natl Acad Sci USA 1998;95:1556-61.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1556-1561
    • Eggeling, C.1    Fries, J.R.2    Brand, L.3    Gunther, R.4    Seidel, C.A.5
  • 36
    • 0014109162 scopus 로고
    • Lipids of human leukocytes: Relation to celltype
    • Gottfried EL. Lipids of human leukocytes: relation to celltype. J Lipid Res 1967;8:321-7.
    • (1967) J Lipid Res , vol.8 , pp. 321-327
    • Gottfried, E.L.1
  • 37
    • 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, et al. 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
  • 38
    • 0029971806 scopus 로고    scopus 로고
    • The transverse location of the fluorescent probe trans-parinaric acid in lipid bilayers
    • Castanho M, Prieto M, Acuna AU. The transverse location of the fluorescent probe trans-parinaric acid in lipid bilayers. Biochim Biophys Acta 1996;1279:164-8.
    • (1996) Biochim Biophys Acta , vol.1279 , pp. 164-168
    • Castanho, M.1    Prieto, M.2    Acuna, A.U.3
  • 39
    • 78649894488 scopus 로고    scopus 로고
    • Quenching of triplet state fluorophores for studying diffusion-mediated reactions in lipid membranes
    • Stromqvist J, Chmyrov A, Johansson S, Andersson A, Maler L, Widengren J. Quenching of triplet state fluorophores for studying diffusion-mediated reactions in lipid membranes. Biophys J 2010;99:3821-30.
    • (2010) Biophys J , vol.99 , pp. 3821-3830
    • Stromqvist, J.1    Chmyrov, A.2    Johansson, S.3    Andersson, A.4    Maler, L.5    Widengren, J.6
  • 40
    • 0041320842 scopus 로고    scopus 로고
    • The distribution of lipid attached spin probes in bilayers: Application to membrane protein topology
    • Vogel A, Scheidt HA, Huster D. The distribution of lipid attached spin probes in bilayers: application to membrane protein topology. Biophys J 2003;85:1691-701.
    • (2003) Biophys J , vol.85 , pp. 1691-1701
    • Vogel, A.1    Scheidt, H.A.2    Huster, D.3
  • 41
    • 0029965541 scopus 로고    scopus 로고
    • A peptide model for calmodulin trapping by calcium/calmodulin-dependent protein kinase II
    • Putkey JA, Waxham MN. A peptide model for calmodulin trapping by calcium/calmodulin-dependent protein kinase II. J Biol Chem 1996;271:29619-23.
    • (1996) J Biol Chem , vol.271 , pp. 29619-29623
    • Putkey, J.A.1    Waxham, M.N.2
  • 42
    • 84877085085 scopus 로고    scopus 로고
    • Calmodulin adopts an extended conformation when interacting with L-selectin in membranes
    • Deng W, Putkey JA, Li R. Calmodulin adopts an extended conformation when interacting with L-selectin in membranes. PLoS One 2013;8:e62861.
    • (2013) PLoS One , vol.8
    • Deng, W.1    Putkey, J.A.2    Li, R.3
  • 43
    • 0022181096 scopus 로고
    • Redistribution of protein kinase C activity in human monocytes: Correlation with activation of the respiratory burst
    • Myers MA, McPhail LC, Snyderman R. Redistribution of protein kinase C activity in human monocytes: correlation with activation of the respiratory burst. J Immunol 1985;135: 3411-6.
    • (1985) J Immunol , vol.135 , pp. 3411-3416
    • Myers, M.A.1    McPhail, L.C.2    Snyderman, R.3
  • 44
    • 0023757217 scopus 로고
    • Function and stimulusspecific effects of phorbol 12-myristate 13-acetate on human polymorphonuclear neutrophils: Autoregulatory role for protein kinase C in signal transduction
    • Smith RJ, Justen JM, Sam LM. Function and stimulusspecific effects of phorbol 12-myristate 13-acetate on human polymorphonuclear neutrophils: autoregulatory role for protein kinase C in signal transduction. Inflammation 1988;12: 597-611.
    • (1988) Inflammation , vol.12 , pp. 597-611
    • Smith, R.J.1    Justen, J.M.2    Sam, L.M.3
  • 45
    • 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, et al. 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
  • 46
    • 70350389704 scopus 로고    scopus 로고
    • ROCK mediates phorbol ester-induced apoptosis in prostate cancer cells via p21Cip1 up-regulation and JNK
    • Xiao L, Eto M, Kazanietz MG. ROCK mediates phorbol ester-induced apoptosis in prostate cancer cells via p21Cip1 up-regulation and JNK. J Biol Chem 2009;284:29365-75.
    • (2009) J Biol Chem , vol.284 , pp. 29365-29375
    • Xiao, L.1    Eto, M.2    Kazanietz, M.G.3
  • 47
    • 0032571406 scopus 로고    scopus 로고
    • Protein kinase C phosphorylation of moesin in the actin-binding sequence
    • Pietromonaco SF, Simons PC, Altman A, Elias L. Protein kinase C phosphorylation of moesin in the actin-binding sequence. J Biol Chem 1998;273:7594-603.
    • (1998) J Biol Chem , vol.273 , pp. 7594-7603
    • Pietromonaco, S.F.1    Simons, P.C.2    Altman, A.3    Elias, L.4
  • 48
    • 0037053360 scopus 로고    scopus 로고
    • RhoA and Rho kinase-dependent phosphorylation of moesin at Thr-558 in hippocampal neuronal cells by glutamate
    • Jeon S, Kim S, Park JB, Suh PG, Kim YS, Bae CD, et al. RhoA and Rho kinase-dependent phosphorylation of moesin at Thr-558 in hippocampal neuronal cells by glutamate. J Biol Chem 2002;277:16576-84.
    • (2002) J Biol Chem , vol.277 , pp. 16576-16584
    • Jeon, S.1    Kim, S.2    Park, J.B.3    Suh, P.G.4    Kim, Y.S.5    Bae, C.D.6
  • 49
    • 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 MR, 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
  • 50
    • 84860857201 scopus 로고    scopus 로고
    • Activation of moesin, a protein that links actin cytoskeleton to the plasma membrane, occurs by phosphatidylinositol 4, 5-bisphosphate (PIP2) binding sequentially to two sites and releasing an autoinhibitory linker
    • Ben-Aissa K, Patino-Lopez G, Belkina NV, Maniti O, Rosales T, Hao JJ, et al. Activation of moesin, a protein that links actin cytoskeleton to the plasma membrane, occurs by phosphatidylinositol 4, 5-bisphosphate (PIP2) binding sequentially to two sites and releasing an autoinhibitory linker. J Biol Chem 2012;287:16311-23.
    • (2012) J Biol Chem , vol.287 , pp. 16311-16323
    • Ben-Aissa, K.1    Patino-Lopez, G.2    Belkina, N.V.3    Maniti, O.4    Rosales, T.5    Hao, J.J.6
  • 51
    • 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 S, Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J 2000;19: 4449-62.
    • (2000) EMBO J , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 52
    • 0034722326 scopus 로고    scopus 로고
    • Mutagenesis of the phosphatidylinositol 4, 5-bisphosphate (PIP2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution
    • Barret C, Roy C, Montcourrier P, Mangeat P, Niggli V. Mutagenesis of the phosphatidylinositol 4, 5-bisphosphate (PIP2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution. J Cell Biol 2000;151:1067-80.
    • (2000) J Cell Biol , vol.151 , pp. 1067-1080
    • Barret, C.1    Roy, C.2    Montcourrier, P.3    Mangeat, P.4    Niggli, V.5
  • 53
    • 84856368235 scopus 로고    scopus 로고
    • Affinity of talin-1 for the β3-integrin cytosolic domain is modulated by its phospholipid bilayer environment
    • Moore DT, Nygren P, Jo H, Boesze-Battaglia K, Bennett JS, DeGrado WF. Affinity of talin-1 for the β3-integrin cytosolic domain is modulated by its phospholipid bilayer environment. Proc Natl Acad Sci USA 2012;109:793-8.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 793-798
    • Moore, D.T.1    Nygren, P.2    Jo, H.3    Boesze-Battaglia, K.4    Bennett, J.S.5    Degrado, W.F.6
  • 54
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 1989;341:456-8.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 55
    • 0033762433 scopus 로고    scopus 로고
    • Phosphorylation of T cell receptor is regulated by a lipid dependent folding transition
    • Aivazian D, Stern LJ. Phosphorylation of T cell receptor is regulated by a lipid dependent folding transition. Nat Struct Biol 2000;7:1023-6.
    • (2000) Nat Struct Biol , vol.7 , pp. 1023-1026
    • Aivazian, D.1    Stern, L.J.2
  • 56
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3å cytoplasmic tyrosine-based motif
    • Xu C, Gagnon E, Call ME, Schnell JR, Schwieters CD, Carman CV, et al. Regulation of T cell receptor activation by dynamic membrane binding of the CD3å cytoplasmic tyrosine-based motif. Cell 2008;135:702-13.
    • (2008) Cell , vol.135 , pp. 702-713
    • Xu, C.1    Gagnon, E.2    Call, M.E.3    Schnell, J.R.4    Schwieters, C.D.5    Carman, C.V.6
  • 57
    • 33750340121 scopus 로고    scopus 로고
    • Structure of the membrane reconstituted transmembranejuxtamembrane peptide EGFR(622-660) and its interaction with Ca2+/calmodulin
    • Sato T, Pallavi P, Golebiewska U, McLaughlin S, Smith SO. Structure of the membrane reconstituted transmembranejuxtamembrane peptide EGFR(622-660) and its interaction with Ca2+/calmodulin. Biochemistry 2006;45:12704-14.
    • (2006) Biochemistry , vol.45 , pp. 12704-12714
    • Sato, T.1    Pallavi, P.2    Golebiewska, U.3    McLaughlin, S.4    Smith, S.O.5
  • 58
    • 33846235429 scopus 로고    scopus 로고
    • Glycoprotein Ibá forms disulfide bonds with 2 glycoprotein Ibß subunits in the resting platelet
    • Luo S-Z, Mo X, Afshar-Kharghan V, Srinivasan S, Lopez JA, Li R. Glycoprotein Ibá forms disulfide bonds with 2 glycoprotein Ibß subunits in the resting platelet. Blood 2007;109:603-9.
    • (2007) Blood , vol.109 , pp. 603-609
    • Luo, S.-Z.1    Mo, X.2    Afshar-Kharghan, V.3    Srinivasan, S.4    Lopez, J.A.5    Li, R.6
  • 59
    • 50049085777 scopus 로고    scopus 로고
    • Specific heteromeric association of four transmembrane peptides derived from platelet glycoprotein Ib-IX complex
    • Luo SZ, Li R. Specific heteromeric association of four transmembrane peptides derived from platelet glycoprotein Ib-IX complex. J Mol Biol 2008;382:448-57.
    • (2008) J Mol Biol , vol.382 , pp. 448-457
    • Luo, S.Z.1    Li, R.2


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