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Volumn 4, Issue , 2013, Pages

Normal muscle regeneration requires tight control of muscle cell fusion by tetraspanins CD9 and CD81

Author keywords

[No Author keywords available]

Indexed keywords

CD81 ANTIGEN; CD9 ANTIGEN;

EID: 84877740791     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2675     Document Type: Article
Times cited : (65)

References (50)
  • 1
    • 0347989458 scopus 로고    scopus 로고
    • Cellular and Molecular Regulation of Muscle Regeneration
    • DOI 10.1152/physrev.00019.2003
    • Charge, S. B. & Rudnicki, M. A. Cellular and molecular regulation of muscle regeneration. Physiol. Rev. 84, 209-238 (2004). (Pubitemid 38049880)
    • (2004) Physiological Reviews , vol.84 , Issue.1 , pp. 209-238
    • Charge, S.B.P.1    Rudnicki, M.A.2
  • 2
    • 22744438723 scopus 로고    scopus 로고
    • Stem cell function, self-renewal, and behavioral heterogeneity of cells from the adult muscle satellite cell niche
    • DOI 10.1016/j.cell.2005.05.010, PII S0092867405004551
    • Collins, C. A. et al. Stem cell function, self-renewal, and behavioral heterogeneity of cells from the adult muscle satellite cell niche. Cell 122, 289-301 (2005). (Pubitemid 41032991)
    • (2005) Cell , vol.122 , Issue.2 , pp. 289-301
    • Collins, C.A.1    Olsen, I.2    Zammit, P.S.3    Heslop, L.4    Petrie, A.5    Partridge, T.A.6    Morgan, J.E.7
  • 3
    • 0034918907 scopus 로고    scopus 로고
    • Myogenic satellite cells: Physiology to molecular biology
    • Hawke, T. J. & Garry, D. J. Myogenic satellite cells: physiology to molecular biology. J. Appl. Physiol. 91, 534-551 (2001). (Pubitemid 32681081)
    • (2001) Journal of Applied Physiology , vol.91 , Issue.2 , pp. 534-551
    • Hawke, T.J.1    Garry, D.J.2
  • 4
    • 84856141914 scopus 로고    scopus 로고
    • Myoblast fusion: Lessons from flies and mice
    • Abmayr, S. M. & Pavlath, G. K. Myoblast fusion: lessons from flies and mice. Development 139, 641-656 (2012).
    • (2012) Development , vol.139 , pp. 641-656
    • Abmayr, S.M.1    Pavlath, G.K.2
  • 5
    • 77951213472 scopus 로고    scopus 로고
    • Myoblast fusion: When it takes more to make one
    • Rochlin, K., Yu, S., Roy, S. & Baylies, M. K. Myoblast fusion: when it takes more to make one. Dev. Biol. 341, 66-83 (2010).
    • (2010) Dev. Biol. , vol.341 , pp. 66-83
    • Rochlin, K.1    Yu, S.2    Roy, S.3    Baylies, M.K.4
  • 7
    • 33746611993 scopus 로고    scopus 로고
    • Mannose receptor regulates myoblast motility and muscle growth
    • DOI 10.1083/jcb.200601102
    • Jansen, K. M. & Pavlath, G. K. Mannose receptor regulates myoblast motility and muscle growth. J. Cell Biol. 174, 403-413 (2006). (Pubitemid 44156770)
    • (2006) Journal of Cell Biology , vol.174 , Issue.3 , pp. 403-413
    • Jansen, K.M.1    Pavlath, G.K.2
  • 8
    • 67749101848 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling regulates the expression of caveolin 3 and beta1 integrin, genes essential for normal myoblast fusion
    • Quach, N. L., Biressi, S., Reichardt, L. F., Keller, C. & Rando, T. A. Focal adhesion kinase signaling regulates the expression of caveolin 3 and beta1 integrin, genes essential for normal myoblast fusion. Mol. Biol. Cell 20, 3422-3435 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3422-3435
    • Quach, N.L.1    Biressi, S.2    Reichardt, L.F.3    Keller, C.4    Rando, T.A.5
  • 9
    • 79954602263 scopus 로고    scopus 로고
    • PKCtheta signaling is required for myoblast fusion by regulating the expression of caveolin-3 and beta1D integrin upstream focal adhesion kinase
    • Madaro, L. et al. PKCtheta signaling is required for myoblast fusion by regulating the expression of caveolin-3 and beta1D integrin upstream focal adhesion kinase. Mol. Biol. Cell 22, 1409-1419 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1409-1419
    • Madaro, L.1
  • 10
    • 79960145986 scopus 로고    scopus 로고
    • New insights into the mechanisms and roles of cell-cell fusion
    • Shinn-Thomas, J. H. & Mohler, W. A. New insights into the mechanisms and roles of cell-cell fusion. Int. Rev. Cell Mol. Biol. 289, 149-209 (2011).
    • (2011) Int. Rev. Cell Mol. Biol. , vol.289 , pp. 149-209
    • Shinn-Thomas, J.H.1    Mohler, W.A.2
  • 11
    • 36448937162 scopus 로고    scopus 로고
    • Cell-to-cell fusion as a link between viruses and cancer
    • DOI 10.1038/nrc2272, PII NRC2272
    • Duelli, D. & Lazebnik, Y. Cell-to-cell fusion as a link between viruses and cancer. Nat. Rev. Cancer 7, 968-976 (2007). (Pubitemid 350165858)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.12 , pp. 968-976
    • Duelli, D.1    Lazebnik, Y.2
  • 12
    • 0033964768 scopus 로고    scopus 로고
    • Severely reduced female fertility in CD9-deficient mice
    • DOI 10.1126/science.287.5451.319
    • Le Naour, F., Rubinstein, E., Jasmin, C., Prenant, M. & Boucheix, C. Severely reduced female fertility in CD9-deficient mice. Science 287, 319-321 (2000). (Pubitemid 30046762)
    • (2000) Science , vol.287 , Issue.5451 , pp. 319-321
    • Boucheix, C.1
  • 16
    • 66549084069 scopus 로고    scopus 로고
    • Lateral organization of membrane proteins: Tetraspanins spin their web
    • Charrin, S. et al. Lateral organization of membrane proteins: tetraspanins spin their web. Biochem. J. 420, 133-154 (2009).
    • (2009) Biochem. J. , vol.420 , pp. 133-154
    • Charrin, S.1
  • 18
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • DOI 10.1038/nrm1736
    • Hemler, M. E. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 6, 801-811 (2005). (Pubitemid 41726118)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.10 , pp. 801-811
    • Hemler, M.E.1
  • 19
    • 0035958026 scopus 로고    scopus 로고
    • The major CD9 and CD81 molecular partner: Identification and characterization of the complexes
    • Charrin, S. et al. The major CD9 and CD81 molecular partner: Identification and characterization of the complexes. J. Biol. Chem. 276, 14329-14337 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 14329-14337
    • Charrin, S.1
  • 21
    • 0035798537 scopus 로고    scopus 로고
    • EWI-2 Is a Major CD9 and CD81 Partner and Member of a Novel Ig Protein Subfamily
    • Stipp, C. S., Kolesnikova, T. V. & Hemler, M. E. EWI-2 Is a Major CD9 and CD81 Partner and Member of a Novel Ig Protein Subfamily. J. Biol. Chem. 276, 40545-40554 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 40545-40554
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 22
    • 0035895876 scopus 로고    scopus 로고
    • FPRP, a major, highly stoichiometric, highly specific CD81-and CD9-associated protein
    • Stipp, C. S., Orlicky, D. & Hemler, M. E. FPRP, a major, highly stoichiometric, highly specific CD81-and CD9-associated protein. J. Biol. Chem. 276, 4853-4862 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4853-4862
    • Stipp, C.S.1    Orlicky, D.2    Hemler, M.E.3
  • 24
    • 0346849708 scopus 로고    scopus 로고
    • EWI-2 regulates α3β1 integrin-dependent cell functions on laminin-5
    • DOI 10.1083/jcb.200309113
    • Stipp, C. S., Kolesnikova, T. V. & Hemler, M. E. EWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-5. J. Cell Biol. 163, 1167-1177 (2003). (Pubitemid 37541891)
    • (2003) Journal of Cell Biology , vol.163 , Issue.5 , pp. 1167-1177
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 25
    • 70450267376 scopus 로고    scopus 로고
    • The Ig domain protein CD9P-1 down-regulates CD81 ability to support Plasmodium yoelii infection
    • Charrin, S. et al. The Ig domain protein CD9P-1 down-regulates CD81 ability to support Plasmodium yoelii infection. J. Biol. Chem. 284, 31572-31578 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 31572-31578
    • Charrin, S.1
  • 26
    • 44849100946 scopus 로고    scopus 로고
    • The CD81 partner EWI-2wint inhibits hepatitis C virus entry
    • Rocha-Perugini, V. et al. The CD81 partner EWI-2wint inhibits hepatitis C virus entry. PLoS ONE 3, e1866 (2008).
    • (2008) PLoS ONE , vol.3
    • Rocha-Perugini, V.1
  • 27
    • 0033598128 scopus 로고    scopus 로고
    • Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
    • DOI 10.1083/jcb.146.4.893
    • Tachibana, I. & Hemler, M. E. Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. J. Cell Biol. 146, 893-904 (1999). (Pubitemid 29408913)
    • (1999) Journal of Cell Biology , vol.146 , Issue.4 , pp. 893-904
    • Tachibana, I.1    Hemler, M.E.2
  • 28
    • 66949172322 scopus 로고    scopus 로고
    • Distinct regulatory cascades govern extraocular and pharyngeal arch muscle progenitor cell fates
    • Sambasivan, R. et al. Distinct regulatory cascades govern extraocular and pharyngeal arch muscle progenitor cell fates. Dev. Cell 16, 810-821 (2009).
    • (2009) Dev. Cell , vol.16 , pp. 810-821
    • Sambasivan, R.1
  • 29
    • 0035963463 scopus 로고    scopus 로고
    • Failure to correct murine muscular dystrophy
    • DOI 10.1038/35082631
    • Ferrari, G., Stornaiuolo, A. & Mavilio, F. Failure to correct murine muscular dystrophy. Nature 411, 1014-1015 (2001). (Pubitemid 32612316)
    • (2001) Nature , vol.411 , Issue.6841 , pp. 1014-1015
    • Ferrari, G.1    Stornaiuolo, A.2    Mavilio, F.3
  • 30
    • 79951552050 scopus 로고    scopus 로고
    • The sarcomeric cytoskeleton: Who picks up the strain?
    • Gautel, M. The sarcomeric cytoskeleton: who picks up the strain? Curr. Opin. Cell Biol. 23, 39-46 (2011).
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 39-46
    • Gautel, M.1
  • 31
    • 45249095633 scopus 로고    scopus 로고
    • Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion
    • DOI 10.1113/jphysiol.2008.151027
    • O'Connor, R. S., Steeds, C. M., Wiseman, R. W. & Pavlath, G. K. Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion. J. Physiol. 586, 2841-2853 (2008). (Pubitemid 351837280)
    • (2008) Journal of Physiology , vol.586 , Issue.12 , pp. 2841-2853
    • O'connor, R.S.1    Steeds, C.M.2    Wiseman, R.W.3    Pavlath, G.K.4
  • 32
    • 70350367763 scopus 로고    scopus 로고
    • Nap1-mediated actin remodeling is essential for mammalian myoblast fusion
    • Nowak, S. J., Nahirney, P. C., Hadjantonakis, A. K. & Baylies, M. K. Nap1-mediated actin remodeling is essential for mammalian myoblast fusion. J. Cell Sci. 122, 3282-3293 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3282-3293
    • Nowak, S.J.1    Nahirney, P.C.2    Hadjantonakis, A.K.3    Baylies, M.K.4
  • 33
    • 0025561020 scopus 로고
    • Fusion between myogenic cells in vivo: An ultrastructural study in regenerating murine skeletal muscle
    • Robertson, T. A., Grounds, M. D., Mitchell, C. A. & Papadimitriou, J. M. Fusion between myogenic cells in vivo: an ultrastructural study in regenerating murine skeletal muscle. J. Struct. Biol. 105, 170-182 (1990).
    • (1990) J. Struct. Biol. , vol.105 , pp. 170-182
    • Robertson, T.A.1    Grounds, M.D.2    Mitchell, C.A.3    Papadimitriou, J.M.4
  • 34
    • 0014406348 scopus 로고
    • The ultrastructural morphology of the muscle fiber in myotonic dystrophy
    • Schroder, J. M. & Adams, R. D. The ultrastructural morphology of the muscle fiber in myotonic dystrophy. Acta Neuropathol. 10, 218-241 (1968).
    • (1968) Acta Neuropathol. , vol.10 , pp. 218-241
    • Schroder, J.M.1    Adams, R.D.2
  • 35
    • 0013931983 scopus 로고
    • Ultrastructural studies of ring fibers in human muscle disease
    • Schotland, D. L., Spiro, D. & Carmel, P. Ultrastructural studies of ring fibers in human muscle disease. J Neuropathol. Exp. Neurol. 25, 431-442 (1966).
    • (1966) J Neuropathol. Exp. Neurol. , vol.25 , pp. 431-442
    • Schotland, D.L.1    Spiro, D.2    Carmel, P.3
  • 36
    • 0029806286 scopus 로고    scopus 로고
    • Cloning, sequencing and proposed structure for a prostglandin F(2α) receptor regulatory protein
    • DOI 10.1016/S0952-3278(96)90007-1
    • Orlicky, D. J. & Nordeen, S. K. Cloning, sequencing and proposed structure for a prostaglandin F2 alpha receptor regulatory protein. Prostaglandins Leukot. Essent. Fatty Acids 55, 261-268 (1996). (Pubitemid 26384204)
    • (1996) Prostaglandins Leukotrienes and Essential Fatty Acids , vol.55 , Issue.4 , pp. 261-268
    • Orlicky, D.J.1    Nordeen, S.K.2
  • 37
    • 0029896396 scopus 로고    scopus 로고
    • Negative regulatory activity of a prostaglandin F(2α) receptor associated protein (FPRP)
    • DOI 10.1016/S0952-3278(96)90055-1
    • Orlicky, D. J. Negative regulatory activity of a prostaglandin F2 alpha receptor associated protein (FPRP). Prostaglandins Leukot. Essent. Fatty Acids 54, 247-259 (1996). (Pubitemid 26201780)
    • (1996) Prostaglandins Leukotrienes and Essential Fatty Acids , vol.54 , Issue.4 , pp. 247-259
    • Orlicky, D.J.1
  • 38
    • 0037437175 scopus 로고    scopus 로고
    • 2α stimulates growth of skeletal muscle cells via an NFATC2-dependent pathway
    • DOI 10.1083/jcb.200208085
    • Horsley, V. & Pavlath, G. K. Prostaglandin F2(alpha) stimulates growth of skeletal muscle cells via an NFATC2-dependent pathway. J. Cell Biol. 161, 111-118 (2003). (Pubitemid 36459084)
    • (2003) Journal of Cell Biology , vol.161 , Issue.1 , pp. 111-118
    • Horsley, V.1    Pavlath, G.K.2
  • 39
    • 24744441713 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR) signaling is required for a late-stage fusion process during skeletal myotube maturation
    • DOI 10.1074/jbc.M506120200
    • Park, I. H. & Chen, J. Mammalian target of rapamycin (mTOR) signaling is required for a late-stage fusion process during skeletal myotube maturation. J. Biol. Chem. 280, 32009-32017 (2005). (Pubitemid 41291952)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 32009-32017
    • Park, I.-H.1    Chen, J.2
  • 40
    • 70449523262 scopus 로고    scopus 로고
    • Analysis of the gamma-secretase interactome and validation of its association with tetraspanin-enriched microdomains
    • Wakabayashi, T. et al. Analysis of the gamma-secretase interactome and validation of its association with tetraspanin-enriched microdomains. Nat. Cell Biol. 11, 1340-1346 (2009).
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1340-1346
    • Wakabayashi, T.1
  • 42
    • 64249172203 scopus 로고    scopus 로고
    • The canonical Notch signaling pathway: Unfolding the activation mechanism
    • Kopan, R. & Ilagan, M. X. The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 137, 216-233 (2009).
    • (2009) Cell , vol.137 , pp. 216-233
    • Kopan, R.1    Ilagan, M.X.2
  • 44
    • 84856118451 scopus 로고    scopus 로고
    • A critical requirement for notch signaling in maintenance of the quiescent skeletal muscle stem cell state
    • Mourikis, P. et al. A critical requirement for notch signaling in maintenance of the quiescent skeletal muscle stem cell state. Stem Cells 30, 243-252 (2012).
    • (2012) Stem Cells , vol.30 , pp. 243-252
    • Mourikis, P.1
  • 46
    • 84864480624 scopus 로고    scopus 로고
    • Tetraspanin-interacting protein IGSF8 is dispensable for mouse fertility
    • Inoue, N., Nishikawa, T., Ikawa, M. & Okabe, M. Tetraspanin- interacting protein IGSF8 is dispensable for mouse fertility. Fertil. Steril. 98, 465-470 (2012).
    • (2012) Fertil. Steril. , vol.98 , pp. 465-470
    • Inoue, N.1    Nishikawa, T.2    Ikawa, M.3    Okabe, M.4
  • 48
    • 0030948267 scopus 로고    scopus 로고
    • Normal lymphocyte development but delayed humoral immune response in CD81-null mice
    • DOI 10.1084/jem.185.8.1505
    • Maecker, H. T. & Levy, S. Normal lymphocyte development but delayed humoral immune response in CD81-null mice. J. Exp. Med. 185, 1505-1510 (1997). (Pubitemid 27187608)
    • (1997) Journal of Experimental Medicine , vol.185 , Issue.8 , pp. 1505-1510
    • Maecker, H.T.1    Levy, S.2
  • 49
    • 0028264320 scopus 로고
    • Primary mouse myoblast purification, characterization, and transplantation for cell-mediated gene therapy
    • DOI 10.1083/jcb.125.6.1275
    • Rando, T. A. & Blau, H. M. Primary mouse myoblast purification, characterization, and transplantation for cell-mediated gene therapy. J. Cell Biol. 125, 1275-1287 (1994). (Pubitemid 24189532)
    • (1994) Journal of Cell Biology , vol.125 , Issue.6 , pp. 1275-1287
    • Rando, T.A.1    Blau, H.M.2


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