메뉴 건너뛰기




Volumn 41, Issue 4, 2011, Pages 1035-1046

The neuronal protein Kidins220/ARMS associates with ICAM-3 and other uropod components and regulates T-cell motility

Author keywords

Cell migration; ICAM 3; Kidins220 ARMS; T cells; Uropod

Indexed keywords

CAVEOLIN 1; INTERCELLULAR ADHESION MOLECULE 3; KIDINS220 ENZYME; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 79953044648     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201040513     Document Type: Article
Times cited : (15)

References (48)
  • 2
    • 0035141510 scopus 로고    scopus 로고
    • An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors
    • Kong, H., Boulter, J., Weber, J. L., Lai, C. and Chao, M. V., An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors. J. Neurosci. 2001. 21: 176-185.
    • (2001) J. Neurosci. , vol.21 , pp. 176-185
    • Kong, H.1    Boulter, J.2    Weber, J.L.3    Lai, C.4    Chao, M.V.5
  • 3
    • 67651055363 scopus 로고    scopus 로고
    • Establishment of axon-dendrite polarity in developing neurons
    • Barnes, A. P. and Polleux, F., Establishment of axon-dendrite polarity in developing neurons. Annu. Rev. Neurosci. 2009. 32: 347-381.
    • (2009) Annu. Rev. Neurosci. , vol.32 , pp. 347-381
    • Barnes, A.P.1    Polleux, F.2
  • 4
    • 56249113020 scopus 로고    scopus 로고
    • The role of the cytoskeleton during neuronal polarization
    • Witte, H. and Bradke, F., The role of the cytoskeleton during neuronal polarization. Curr. Opin. Neurobiol. 2008. 18: 479-487.
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 479-487
    • Witte, H.1    Bradke, F.2
  • 5
    • 74049151120 scopus 로고    scopus 로고
    • Kidins220/ARMS modulates the activity of microtubule-regulating proteins and controls neuronal polarity and development
    • Higuero, A. M., Sanchez-Ruiloba, L., Doglio, L. E., Portillo, F., Abad-Rodriguez, J., Dotti, C. G. and Iglesias, T., Kidins220/ARMS modulates the activity of microtubule-regulating proteins and controls neuronal polarity and development. J. Biol. Chem. 2008. 285: 1343-1357.
    • (2008) J. Biol. Chem , vol.285 , pp. 1343-1357
    • Higuero, A.M.1    Sanchez-Ruiloba, L.2    Doglio, L.E.3    Portillo, F.4    Abad-Rodriguez, J.5    Dotti, C.G.6    Iglesias, T.7
  • 6
    • 0033019133 scopus 로고    scopus 로고
    • Cytoskeletal rearrangement during migration and activation of T lymphocytes
    • Serrador, J. M., Nieto, M. and Sanchez-Madrid, F., Cytoskeletal rearrangement during migration and activation of T lymphocytes. Trends Cell. Biol. 1999. 9: 228-233.
    • (1999) Trends Cell. Biol. , vol.9 , pp. 228-233
    • Serrador, J.M.1    Nieto, M.2    Sanchez-Madrid, F.3
  • 7
    • 0033215149 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositol 3-kinase in stromal cell-derived factor-1 alpha-induced lymphocyte polarization and chemotaxis
    • Vicente-Manzanares, M., Rey, M., Jones, D. R., Sancho, D., Mellado, M., Rodriguez-Frade, J. M., del Pozo, M. A. et al., Involvement of phosphatidylinositol 3-kinase in stromal cell-derived factor-1 alpha-induced lymphocyte polarization and chemotaxis. J. Immunol. 1999. 163: 4001-4012.
    • (1999) J. Immunol. , vol.163 , pp. 4001-4012
    • Vicente-Manzanares, M.1    Rey, M.2    Jones, D.R.3    Sancho, D.4    Mellado, M.5    Rodriguez-Frade, J.M.6    del Pozo, M.A.7
  • 8
    • 0242683360 scopus 로고    scopus 로고
    • Leukocyte polarization in cell migration and immune interactions
    • Sanchez-Madrid, F. and del Pozo, M. A., Leukocyte polarization in cell migration and immune interactions. EMBO J. 1999. 18: 501-511.
    • (1999) EMBO J. , vol.18 , pp. 501-511
    • Sanchez-Madrid, F.1    del Pozo, M.A.2
  • 10
    • 0028148556 scopus 로고
    • ICAM-3 regulates lymphocyte morphology and integrin-mediated T cell interaction with endothelial cell and extracellular matrix ligands
    • Campanero, M. R., Sanchez-Mateos, P., del Pozo, M. A. and Sanchez-Madrid, F., ICAM-3 regulates lymphocyte morphology and integrin-mediated T cell interaction with endothelial cell and extracellular matrix ligands. J. Cell. Biol. 1994. 127: 867-878.
    • (1994) J. Cell. Biol. , vol.127 , pp. 867-878
    • Campanero, M.R.1    Sanchez-Mateos, P.2    del Pozo, M.A.3    Sanchez-Madrid, F.4
  • 12
    • 0030785793 scopus 로고    scopus 로고
    • Polarization of chemokine receptors to the leading edge during lymphocyte chemotaxis
    • Nieto, M., Frade, J. M., Sancho, D., Mellado, M., Martinez, A. C. and Sanchez-Madrid, F., Polarization of chemokine receptors to the leading edge during lymphocyte chemotaxis. J. Exp. Med. 1997. 186: 153-158.
    • (1997) J. Exp. Med. , vol.186 , pp. 153-158
    • Nieto, M.1    Frade, J.M.2    Sancho, D.3    Mellado, M.4    Martinez, A.C.5    Sanchez-Madrid, F.6
  • 13
    • 0028863513 scopus 로고
    • Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix. Involvement of cAMP signaling pathway
    • del Pozo, M. A., Sanchez-Mateos, P., Nieto, M. and Sanchez-Madrid, F., Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix. Involvement of cAMP signaling pathway. J. Cell. Biol. 1995. 131: 495-508.
    • (1995) J. Cell. Biol. , vol.131 , pp. 495-508
    • del Pozo, M.A.1    Sanchez-Mateos, P.2    Nieto, M.3    Sanchez-Madrid, F.4
  • 15
    • 0036464668 scopus 로고    scopus 로고
    • Lipid rafts mediate biosynthetic transport to the T lymphocyte uropod subdomain and are necessary for uropod integrity and function
    • Millan, J., Montoya, M. C., Sancho, D., Sanchez-Madrid, F. and Alonso, M. A., Lipid rafts mediate biosynthetic transport to the T lymphocyte uropod subdomain and are necessary for uropod integrity and function. Blood 2002. 99: 978-984.
    • (2002) Blood , vol.99 , pp. 978-984
    • Millan, J.1    Montoya, M.C.2    Sancho, D.3    Sanchez-Madrid, F.4    Alonso, M.A.5
  • 17
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita, S., Oishi, K., Sato, N., Sagara, J., Kawai, A. and Tsukita, S., ERM family members as molecular 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
  • 18
    • 0031043523 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction
    • Tsukita, S. and Yonemura, S., ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. Curr. Opin. Cell. Biol. 1997. 9: 70-75.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 70-75
    • Tsukita, S.1    Yonemura, S.2
  • 19
    • 67349256860 scopus 로고    scopus 로고
    • Bringing up the rear: defining the roles of the uropod
    • Sanchez-Madrid, F. and Serrador, J. M., Bringing up the rear: defining the roles of the uropod. Nat. Rev. Mol. Cell. Biol. 2009. 10: 353-359.
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 353-359
    • Sanchez-Madrid, F.1    Serrador, J.M.2
  • 21
    • 3142582003 scopus 로고    scopus 로고
    • Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells
    • Cabrera-Poch, N., Sanchez-Ruiloba, L., Rodriguez-Martinez, M. and Iglesias, T., Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells. J. Biol. Chem. 2004. 279: 28592-28602.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28592-28602
    • Cabrera-Poch, N.1    Sanchez-Ruiloba, L.2    Rodriguez-Martinez, M.3    Iglesias, T.4
  • 23
    • 0037306407 scopus 로고    scopus 로고
    • The roles of membrane microdomains (rafts) in T cell activation
    • Horejsi, V., The roles of membrane microdomains (rafts) in T cell activation. Immunol. Rev. 2003. 191: 148-164.
    • (2003) Immunol. Rev. , vol.191 , pp. 148-164
    • Horejsi, V.1
  • 24
    • 0037716812 scopus 로고    scopus 로고
    • Lymphocyte lipid rafts: structure and function
    • Pizzo, P. and Viola, A., Lymphocyte lipid rafts: structure and function. Curr. Opin. Immunol. 2003. 15: 255-260.
    • (2003) Curr. Opin. Immunol. , vol.15 , pp. 255-260
    • Pizzo, P.1    Viola, A.2
  • 26
    • 33644626451 scopus 로고    scopus 로고
    • Differential-expression and tyrosine-phosphorylation profiles of caveolin isoforms in human T cell leukemia cell lines
    • Tsuji, Y., Hatanaka, M., Maeda, T., Seya, T., Takenaka, H. and Shimizu, A., Differential-expression and tyrosine-phosphorylation profiles of caveolin isoforms in human T cell leukemia cell lines. Int. J. Mol. Med. 2005. 16: 889-893.
    • (2005) Int. J. Mol. Med. , vol.16 , pp. 889-893
    • Tsuji, Y.1    Hatanaka, M.2    Maeda, T.3    Seya, T.4    Takenaka, H.5    Shimizu, A.6
  • 30
    • 4444245423 scopus 로고    scopus 로고
    • Protein kinase C and beyond
    • Spitaler, M. and Cantrell, D. A., Protein kinase C and beyond. Nat. Immunol. 2004. 5: 785-790.
    • (2004) Nat. Immunol. , vol.5 , pp. 785-790
    • Spitaler, M.1    Cantrell, D.A.2
  • 31
    • 0030939803 scopus 로고    scopus 로고
    • ICAMs redistributed by chemokines to cellular uropods as a mechanism for recruitment of T lymphocytes
    • del Pozo, M. A., Cabanas, C., Montoya, M. C., Ager, A., Sanchez-Mateos, P. and Sanchez-Madrid, F., ICAMs redistributed by chemokines to cellular uropods as a mechanism for recruitment of T lymphocytes. J. Cell. Biol. 1997. 137: 493-508.
    • (1997) J. Cell. Biol. , vol.137 , pp. 493-508
    • del Pozo, M.A.1    Cabanas, C.2    Montoya, M.C.3    Ager, A.4    Sanchez-Mateos, P.5    Sanchez-Madrid, F.6
  • 33
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin
    • Fra, A. M., Williamson, E., Simons, K. and Parton, R. G., De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc. Natl. Acad. Sci. USA 1995. 92: 8655-8659.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 34
    • 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, J. M., Alonso-Lebrero, J. L., del Pozo, M. A., Furthmayr, H., Schwartz-Albiez, R., Calvo, J., Lozano, F. and 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 polarization. J. Cell. Biol. 1997. 138: 1409-1423.
    • (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    Lozano, F.7    Sanchez-Madrid, F.8
  • 35
    • 0031838741 scopus 로고    scopus 로고
    • CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts
    • Serrador, J. M., Nieto, M., Alonso-Lebrero, J. L., del Pozo, M. A., Calvo, J., Furthmayr, H., Schwartz-Albiez, R. et al., CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. Blood 1998. 91: 4632-4644.
    • (1998) Blood , vol.91 , pp. 4632-4644
    • Serrador, J.M.1    Nieto, M.2    Alonso-Lebrero, J.L.3    del Pozo, M.A.4    Calvo, J.5    Furthmayr, H.6    Schwartz-Albiez, R.7
  • 36
    • 7244247060 scopus 로고    scopus 로고
    • Roles of p-ERM and Rho-ROCK signaling in lymphocyte polarity and uropod formation
    • Lee, J. H., Katakai, T., Hara, T., Gonda, H., Sugai, M. and Shimizu, A., Roles of p-ERM and Rho-ROCK signaling in lymphocyte polarity and uropod formation. J. Cell. Biol. 2004. 167: 327-337.
    • (2004) J. Cell. Biol. , vol.167 , pp. 327-337
    • Lee, J.H.1    Katakai, T.2    Hara, T.3    Gonda, H.4    Sugai, M.5    Shimizu, A.6
  • 37
    • 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. and 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: 885-895.
    • (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    Tsukita, S.7
  • 38
    • 2542588542 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes
    • Ivetic, A. and Ridley, A. J., Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes. Immunology 2004. 112: 165-176.
    • (2004) Immunology , vol.112 , pp. 165-176
    • Ivetic, A.1    Ridley, A.J.2
  • 39
    • 22344445407 scopus 로고    scopus 로고
    • {Alpha} -syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner
    • Luo, S., Chen, Y., Lai, K. O., Arevalo, J. C., Froehner, S. C., Adams, M. E., Chao, M. V. and Ip, N. Y., {Alpha} -syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner. J. Cell. Biol. 2005. 169: 813-824.
    • (2005) J. Cell. Biol. , vol.169 , pp. 813-824
    • Luo, S.1    Chen, Y.2    Lai, K.O.3    Arevalo, J.C.4    Froehner, S.C.5    Adams, M.E.6    Chao, M.V.7    Ip, N.Y.8
  • 40
    • 33745815978 scopus 로고    scopus 로고
    • Protein kinase D intracellular localization and activity control kinase D-interacting substrate of 220-kDa traffic through a postsynaptic density-95/discs large/zonula occludens-1-binding motif
    • Sanchez-Ruiloba, L., Cabrera-Poch, N., Rodriguez-Martinez, M., Lopez-Menendez, C., Jean-Mairet, R. M., Higuero, A. M. and Iglesias, T., Protein kinase D intracellular localization and activity control kinase D-interacting substrate of 220-kDa traffic through a postsynaptic density-95/discs large/zonula occludens-1-binding motif. J. Biol. Chem. 2006. 281: 18888-18900.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18888-18900
    • Sanchez-Ruiloba, L.1    Cabrera-Poch, N.2    Rodriguez-Martinez, M.3    Lopez-Menendez, C.4    Jean-Mairet, R.M.5    Higuero, A.M.6    Iglesias, T.7
  • 41
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • Reczek, D., Berryman, M. and Bretscher, A., Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J. Cell. Biol. 1997. 139: 169-179.
    • (1997) J. Cell. Biol. , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 42
  • 43
    • 0034524664 scopus 로고    scopus 로고
    • ERM-Merlin and EBP50 protein families in plasma membrane organization and function
    • Bretscher, A., Chambers, D., Nguyen, R. and Reczek, D., ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu. Rev. Cell. Dev. Biol. 2000. 16: 113-143.
    • (2000) Annu. Rev. Cell. Dev. Biol. , vol.16 , pp. 113-143
    • Bretscher, A.1    Chambers, D.2    Nguyen, R.3    Reczek, D.4
  • 44
    • 0030803795 scopus 로고    scopus 로고
    • Functional mapping of the cytoplasmic region of intercellular adhesion molecule-3 reveals important roles for serine residues
    • Hayflick, J. S., Stine, J., Fox, R., Hoekstra, D. and Gallatin, W. M., Functional mapping of the cytoplasmic region of intercellular adhesion molecule-3 reveals important roles for serine residues. J. Biol. Chem. 1997. 272: 22207-22214.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22207-22214
    • Hayflick, J.S.1    Stine, J.2    Fox, R.3    Hoekstra, D.4    Gallatin, W.M.5
  • 45
    • 0037155885 scopus 로고    scopus 로고
    • A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting
    • Serrador, J. M., Vicente-Manzanares, M., Calvo, J., Barreiro, O., Montoya, M. C., Schwartz-Albiez, R., Furthmayr, H. et al., A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting. J. Biol. Chem. 2002. 277: 10400-10409.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10400-10409
    • Serrador, J.M.1    Vicente-Manzanares, M.2    Calvo, J.3    Barreiro, O.4    Montoya, M.C.5    Schwartz-Albiez, R.6    Furthmayr, H.7
  • 46
    • 0032571406 scopus 로고    scopus 로고
    • Protein kinase C-theta phosphorylation of moesin in the actin-binding sequence
    • Pietromonaco, S. F., Simons, P. C., Altman, A. and Elias, L., Protein kinase C-theta phosphorylation of moesin in the actin-binding sequence. J. Biol. Chem. 1998. 273: 7594-7603.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7594-7603
    • Pietromonaco, S.F.1    Simons, P.C.2    Altman, A.3    Elias, L.4
  • 47
    • 0033543570 scopus 로고    scopus 로고
    • Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/Protein kinase Cmu
    • Matthews, S. A., Rozengurt, E. and Cantrell, D., Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/Protein kinase Cmu. J. Biol. Chem. 1999. 274: 26543-26549.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26543-26549
    • Matthews, S.A.1    Rozengurt, E.2    Cantrell, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.