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Volumn 30, Issue 6, 2015, Pages 438-448

Plasma membrane repair: A central process for maintaining cellular homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 84946414869     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00019.2015     Document Type: Review
Times cited : (92)

References (143)
  • 1
    • 33344455688 scopus 로고    scopus 로고
    • Intracellular localization of dysferlin and its association with the dihydropyridine receptor
    • Ampong BN, Imamura M, Matsumiya T, Yoshida M, Takeda S. Intracellular localization of dysferlin and its association with the dihydropyridine receptor. Acta Myol 24: 134-144, 2005
    • (2005) Acta Myol , vol.24 , pp. 134-144
    • Ampong, B.N.1    Imamura, M.2    Matsumiya, T.3    Yoshida, M.4    Takeda, S.5
  • 3
    • 0034605044 scopus 로고    scopus 로고
    • Annexins in cell membrane dynamics. Ca2_-regulated association of lipid microdomains
    • Babiychuk EB, Draeger A. Annexins in cell membrane dynamics. Ca2_-regulated association of lipid microdomains. J Cell Biol 150: 1113-1124, 2000
    • (2000) J Cell Biol , vol.150 , pp. 1113-1124
    • Babiychuk, E.B.1    Draeger, A.2
  • 4
    • 67650760385 scopus 로고    scopus 로고
    • Intracellular Ca2_ operates a switch between repair and lysis of streptolysin O-perforated cells
    • Babiychuk EB, Monastyrskaya K, Potez S, Draeger A. Intracellular Ca2_ operates a switch between repair and lysis of streptolysin O-perforated cells. Cell Death Differ 16: 1126-1134, 2009
    • (2009) Cell Death Differ , vol.16 , pp. 1126-1134
    • Babiychuk, E.B.1    Monastyrskaya, K.2    Potez, S.3    Draeger, A.4
  • 7
    • 29744433636 scopus 로고    scopus 로고
    • Brain response to injury and neurodegeneration: Endogenous neuroprotective signaling
    • Bazan NG, Marcheselli VL, Cole-Edwards K. Brain response to injury and neurodegeneration: endogenous neuroprotective signaling. Ann NY Acad Sci 1053: 137-147, 2005
    • (2005) Ann NY Acad Sci , vol.1053 , pp. 137-147
    • Bazan, N.G.1    Marcheselli, V.L.2    Cole-Edwards, K.3
  • 8
    • 56949085969 scopus 로고    scopus 로고
    • Calpain 3, the “gatekeeper” of proper sarcomere assembly, turnover and maintenance
    • Beckmann JS, Spencer M. Calpain 3, the “gatekeeper” of proper sarcomere assembly, turnover and maintenance. Neuromuscul Disord 18: 913-921, 2008
    • (2008) Neuromuscul Disord , vol.18 , pp. 913-921
    • Beckmann, J.S.1    Spencer, M.2
  • 9
    • 0027176798 scopus 로고
    • A novel cytoskeletal structure involved in purse string wound closure and cell polarity maintenance
    • Bement WM, Forscher P, Mooseker MS. A novel cytoskeletal structure involved in purse string wound closure and cell polarity maintenance. J Cell Biol 121: 565-578, 1993
    • (1993) J Cell Biol , vol.121 , pp. 565-578
    • Bement, W.M.1    Forscher, P.2    Mooseker, M.S.3
  • 10
    • 0347753248 scopus 로고    scopus 로고
    • AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture
    • Benaud C, Gentil BJ, Assard N, Court M, Garin J, Delphin C, Baudier J. AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture. J Cell Biol 164: 133-144, 2004
    • (2004) J Cell Biol , vol.164 , pp. 133-144
    • Benaud, C.1    Gentil, B.J.2    Assard, N.3    Court, M.4    Garin, J.5    Delphin, C.6    Baudier, J.7
  • 12
    • 0029609143 scopus 로고
    • Calcium-regulated exocytosis is required for cell membrane resealing
    • Bi GQ, Alderton JM, Steinhardt RA. Calcium-regulated exocytosis is required for cell membrane resealing. J Cell Biol 131: 1747-1758, 1995
    • (1995) J Cell Biol , vol.131 , pp. 1747-1758
    • Bi, G.Q.1    Alderton, J.M.2    Steinhardt, R.A.3
  • 13
    • 0027269605 scopus 로고
    • Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis
    • Bommert K, Charlton MP, DeBello WM, Chin GJ, Betz H, Augustine GJ. Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis. Nature 363: 163-165, 1993
    • (1993) Nature , vol.363 , pp. 163-165
    • Bommert, K.1    Charlton, M.P.2    Debello, W.M.3    Chin, G.J.4    Betz, H.5    Augustine, G.J.6
  • 16
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose N, Petrenko AG, Südhof TC, Jahn R. Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science 256: 1021-1025, 1992
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Südhof, T.C.3    Jahn, R.4
  • 20
    • 67650133653 scopus 로고    scopus 로고
    • Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin
    • Cai C, Weisleder N, Ko JK, Komazaki S, Sunada Y, Nishi M, Takeshima H, Ma J. Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin. J Biol Chem 284: 15894-15902, 2009
    • (2009) J Biol Chem , vol.284 , pp. 15894-15902
    • Cai, C.1    Weisleder, N.2    Ko, J.K.3    Komazaki, S.4    Sunada, Y.5    Nishi, M.6    Takeshima, H.7    Ma, J.8
  • 23
    • 84946425195 scopus 로고
    • Explorations into the nature of the living cell
    • Chambers R, Chambers EL. Explorations into the nature of the living cell. Acad Med 36: 966, 1961
    • (1961) Acad Med , vol.36
    • Chambers, R.1    Chambers, E.L.2
  • 24
    • 73549116514 scopus 로고    scopus 로고
    • Dysferlin deficiency and the development of cardiomyopathy in a mouse model of limb-girdle muscular dystrophy 2B
    • Chase TH, Cox GA, Burzenski L, Foreman O, Shultz LD. Dysferlin deficiency and the development of cardiomyopathy in a mouse model of limb-girdle muscular dystrophy 2B. Am J Pathol 175: 2299-2308, 2009
    • (2009) Am J Pathol , vol.175 , pp. 2299-2308
    • Chase, T.H.1    Cox, G.A.2    Burzenski, L.3    Foreman, O.4    Shultz, L.D.5
  • 25
    • 0023636677 scopus 로고
    • Biomembrane fusion: A new concept derived from model studies using two interacting planar lipid bilayers
    • Chernomordik LV, Melikyan GB, Chizmadzhev YA. Biomembrane fusion: a new concept derived from model studies using two interacting planar lipid bilayers. Biochim Biophys Acta 906: 309-352, 1987
    • (1987) Biochim Biophys Acta , vol.906 , pp. 309-352
    • Chernomordik, L.V.1    Melikyan, G.B.2    Chizmadzhev, Y.A.3
  • 27
    • 34047177492 scopus 로고    scopus 로고
    • Dystrophinopathy carrier determination and detection of protein deficiencies in muscular dystrophy using lentiviral MyoD-forced myogenesis
    • Cooper ST, Kizana E, Yates JD, Lo HP, Yang N, Wu ZH, Alexander IE, North KN. Dystrophinopathy carrier determination and detection of protein deficiencies in muscular dystrophy using lentiviral MyoD-forced myogenesis. Neuromuscul Disord 17: 276-284, 2007
    • (2007) Neuromuscul Disord , vol.17 , pp. 276-284
    • Cooper, S.T.1    Kizana, E.2    Yates, J.D.3    Lo, H.P.4    Yang, N.5    Wu, Z.H.6    Alexander, I.E.7    North, K.N.8
  • 28
    • 84900500504 scopus 로고    scopus 로고
    • Effect of recombinant human MG53 protein on tourniquet-induced ischemiareperfusion injury in rat muscle
    • Corona BT, Garg K, Roe JL, Zhu H, Park KH, Ma J, Walters TJ. Effect of recombinant human MG53 protein on tourniquet-induced ischemiareperfusion injury in rat muscle. Muscle Nerve 49: 919-921, 2014
    • (2014) Muscle Nerve , vol.49 , pp. 919-921
    • Corona, B.T.1    Garg, K.2    Roe, J.L.3    Zhu, H.4    Park, K.H.5    Ma, J.6    Walters, T.J.7
  • 30
    • 84856787672 scopus 로고    scopus 로고
    • Toxin pores endocytosed during plasma membrane repair traffic into the lumen of MVBs for degradation
    • Corrotte M, Fernandes MC, Tam C, Andrews NW. Toxin pores endocytosed during plasma membrane repair traffic into the lumen of MVBs for degradation. Traffic 13: 483-494, 2012
    • (2012) Traffic , vol.13 , pp. 483-494
    • Corrotte, M.1    Fernandes, M.C.2    Tam, C.3    Rews, N.W.4
  • 31
    • 77953142289 scopus 로고    scopus 로고
    • Membrane wounding triggers ATP release and dysferlin-mediated intercellular calcium signaling
    • Covian-Nares JF, Koushik SV, Puhl HL, Vogel SS. Membrane wounding triggers ATP release and dysferlin-mediated intercellular calcium signaling. J Cell Sci 123: 1884-1893, 2010
    • (2010) J Cell Sci , vol.123 , pp. 1884-1893
    • Covian-Nares, J.F.1    Koushik, S.V.2    Puhl, H.L.3    Vogel, S.S.4
  • 32
    • 0033213302 scopus 로고    scopus 로고
    • Kinetics of synaptotagmin responses to Ca2_ and assembly with the core SNARE complex onto membranes
    • Davis AF, Bai J, Fasshauer D, Wolowick MJ, Lewis JL, Chapman ER. Kinetics of synaptotagmin responses to Ca2_ and assembly with the core SNARE complex onto membranes. Neuron 24: 363-376, 1999
    • (1999) Neuron , vol.24 , pp. 363-376
    • Davis, A.F.1    Bai, J.2    Fasshauer, D.3    Wolowick, M.J.4    Lewis, J.L.5    Chapman, E.R.6
  • 36
    • 78751683605 scopus 로고    scopus 로고
    • Impaired muscle growth and response to insulin-like growth factor 1 in dysferlin-mediated muscular dystrophy
    • Demonbreun AR, Fahrenbach JP, Deveaux K, Earley JU, Pytel P, McNally EM. Impaired muscle growth and response to insulin-like growth factor 1 in dysferlin-mediated muscular dystrophy. Hum Mol Genet 20: 779-789, 2011
    • (2011) Hum Mol Genet , vol.20 , pp. 779-789
    • Demonbreun, A.R.1    Fahrenbach, J.P.2    Deveaux, K.3    Earley, J.U.4    Pytel, P.5    McNally, E.M.6
  • 38
    • 84867403720 scopus 로고    scopus 로고
    • Structure of an asymmetric ternary protein complex provides insight for membrane interaction
    • Dempsey BR, Rezvanpour A, Lee TW, Barber KR, Junop MS, Shaw GS. Structure of an asymmetric ternary protein complex provides insight for membrane interaction. Structure 20: 1737-1745, 2012
    • (2012) Structure , vol.20 , pp. 1737-1745
    • Dempsey, B.R.1    Rezvanpour, A.2    Lee, T.W.3    Barber, K.R.4    Junop, M.S.5    Shaw, G.S.6
  • 39
    • 34249794279 scopus 로고    scopus 로고
    • New insights into membrane trafficking and protein sorting
    • Derby MC, Gleeson PA. New insights into membrane trafficking and protein sorting. Intl Rev Cytol 261: 47-116, 2007
    • (2007) Intl Rev Cytol , vol.261 , pp. 47-116
    • Derby, M.C.1    Gleeson, P.A.2
  • 43
    • 79951952737 scopus 로고    scopus 로고
    • Plasma membrane repair and cellular damage control: The annexin survival kit
    • Draeger A, Monastyrskaya K, Babiychuk EB. Plasma membrane repair and cellular damage control: the annexin survival kit. Biochem Pharmacol 81: 703-712, 2011
    • (2011) Biochem Pharmacol , vol.81 , pp. 703-712
    • Draeger, A.1    Monastyrskaya, K.2    Babiychuk, E.B.3
  • 45
    • 33746129198 scopus 로고    scopus 로고
    • Calpain 3: A key regulator of the sarcomere?
    • Duguez S, Bartoli M, Richard I. Calpain 3: a key regulator of the sarcomere? FEBS J 273: 3427-3436, 2006
    • (2006) FEBS J , vol.273 , pp. 3427-3436
    • Duguez, S.1    Bartoli, M.2    Richard, I.3
  • 46
    • 0035904238 scopus 로고    scopus 로고
    • The tandem C2 domains of synaptotagmin contain redundant Ca2_ binding sites that cooperate to engage t-SNAREs and trigger exocytosis
    • Earles CA, Bai J, Wang P, Chapman ER. The tandem C2 domains of synaptotagmin contain redundant Ca2_ binding sites that cooperate to engage t-SNAREs and trigger exocytosis. J Cell Biol 154: 1117-1123, 2001
    • (2001) J Cell Biol , vol.154 , pp. 1117-1123
    • Earles, C.A.1    Bai, J.2    Wang, P.3    Chapman, E.R.4
  • 47
    • 77956542690 scopus 로고    scopus 로고
    • Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway
    • Evesson FJ, Peat RA, Lek A, Brilot F, Lo HP, Dale RC, Parton RG, North KN, Cooper ST. Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway. J Biol Chem 285: 28529-28539, 2010
    • (2010) J Biol Chem , vol.285 , pp. 28529-28539
    • Evesson, F.J.1    Peat, R.A.2    Lek, A.3    Brilot, F.4    Lo, H.P.5    Dale, R.C.6    Parton, R.G.7    North, K.N.8    Cooper, S.T.9
  • 48
    • 34447648009 scopus 로고    scopus 로고
    • Synaptotagmin I and II are present in distinct subsets of central synapses
    • Fox MA, Sanes JR. Synaptotagmin I and II are present in distinct subsets of central synapses. J Comp Neurol 503: 280-296, 2007
    • (2007) J Comp Neurol , vol.503 , pp. 280-296
    • Fox, M.A.1    Sanes, J.R.2
  • 49
    • 0028832353 scopus 로고
    • Role of the C2B domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal
    • Fukuda M, Moreira JE, Lewis FM, Sugimori M, Niinobe M, Mikoshiba K, Llinás R. Role of the C2B domain of synaptotagmin in vesicular release and recycling as determined by specific antibody injection into the squid giant synapse preterminal. Proc Natl Acad Sci USA 92: 10708-10712, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10708-10712
    • Fukuda, M.1    Moreira, J.E.2    Lewis, F.M.3    Sugimori, M.4    Niinobe, M.5    Mikoshiba, K.6    Llinás, R.7
  • 52
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion
    • Geppert M, Goda Y, Stevens CF, Südhof TC. The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. Nature 387: 810-814, 1997
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1    Goda, Y.2    Stevens, C.F.3    Südhof, T.C.4
  • 53
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca2_ signalling to membrane dynamics
    • Gerke V, Creutz CE, Moss SE. Annexins: linking Ca2_ signalling to membrane dynamics. Nat Rev Mol Cell Biol 6: 449-461, 2005
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 54
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke V, Moss SE. Annexins: from structure to function. Physiol Rev 82: 331-371, 2002
    • (2002) Physiol Rev , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 55
    • 84877923964 scopus 로고    scopus 로고
    • Compensation of the AKT signaling by ERK signaling in transgenic mice hearts overexpressing TRIM72
    • Ham YM, Mahoney SJ. Compensation of the AKT signaling by ERK signaling in transgenic mice hearts overexpressing TRIM72. Exp Cell Res 319: 1451-1462, 2013
    • (2013) Exp Cell Res , vol.319 , pp. 1451-1462
    • Ham, Y.M.1    Mahoney, S.J.2
  • 56
    • 34447118089 scopus 로고    scopus 로고
    • Dysferlin-mediated membrane repair protects the heart from stressinduced left ventricular injury
    • Han R, Bansal D, Miyake K, Muniz VP, Weiss RM, McNeil PL, Campbell KP. Dysferlin-mediated membrane repair protects the heart from stressinduced left ventricular injury. J Clin Invest 117: 1805-1813, 2007
    • (2007) J Clin Invest , vol.117 , pp. 1805-1813
    • Han, R.1    Bansal, D.2    Miyake, K.3    Muniz, V.P.4    Weiss, R.M.5    McNeil, P.L.6    Campbell, K.P.7
  • 57
    • 34548009359 scopus 로고    scopus 로고
    • Dysferlin and muscle membrane repair
    • Han R, Campbell KP. Dysferlin and muscle membrane repair. Curr Opin Cell Biol 19: 409-416, 2007
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 409-416
    • Han, R.1    Campbell, K.P.2
  • 64
    • 0034087155 scopus 로고    scopus 로고
    • Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes
    • Holopainen JM, Angelova MI, Kinnunen PK. Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes. Biophys J 78: 830-838, 2000
    • (2000) Biophys J , vol.78 , pp. 830-838
    • Holopainen, J.M.1    Angelova, M.I.2    Kinnunen, P.K.3
  • 65
    • 0034625410 scopus 로고    scopus 로고
    • A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis
    • Holz RW, Hlubek MD, Sorensen SD, Fisher SK, Balla T, Ozaki S, Prestwich GD, Stuenkel EL, Bittner MA. A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis. J Biol Chem 275: 17878-17885, 2000
    • (2000) J Biol Chem , vol.275 , pp. 17878-17885
    • Holz, R.W.1    Hlubek, M.D.2    Sorensen, S.D.3    Fisher, S.K.4    Balla, T.5    Ozaki, S.6    Prestwich, G.D.7    Stuenkel, E.L.8    Bittner, M.A.9
  • 66
    • 1642358909 scopus 로고    scopus 로고
    • Activation of m-calpain is required for chromosome alignment on the metaphase plate during mitosis
    • Honda S, Marumoto T, Hirota T, Nitta M, Arima Y, Ogawa M, Saya H. Activation of m-calpain is required for chromosome alignment on the metaphase plate during mitosis. J Biol Chem 279: 10615-10623, 2004
    • (2004) J Biol Chem , vol.279 , pp. 10615-10623
    • Honda, S.1    Marumoto, T.2    Hirota, T.3    Nitta, M.4    Arima, Y.5    Ogawa, M.6    Saya, H.7
  • 69
    • 79959857021 scopus 로고    scopus 로고
    • Redox-dependent oligomerization through a leucine zipper motif is essential for MG53-mediated cell membrane repair
    • Hwang M, Ko JK, Weisleder N, Takeshima H, Ma J. Redox-dependent oligomerization through a leucine zipper motif is essential for MG53-mediated cell membrane repair. Am J Physiol Cell Physiol 301: C106-C114, 2011
    • (2011) Am J Physiol Cell Physiol , vol.301 , pp. C106-C114
    • Hwang, M.1    Ko, J.K.2    Weisleder, N.3    Takeshima, H.4    Ma, J.5
  • 70
    • 40849118150 scopus 로고    scopus 로고
    • Repair of injured plasma membrane by rapid Ca2_-dependent endocytosis
    • Idone V, Tam C, Goss JW, Toomre D, Pypaert M, Andrews NW. Repair of injured plasma membrane by rapid Ca2_-dependent endocytosis. J Cell Biol 180: 905-914, 2008
    • (2008) J Cell Biol , vol.180 , pp. 905-914
    • Idone, V.1    Tam, C.2    Goss, J.W.3    Toomre, D.4    Pypaert, M.5    Rews, N.W.6
  • 75
    • 77957731333 scopus 로고    scopus 로고
    • Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion
    • Johnson CP, Chapman ER. Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion. J Cell Biol 191: 187-197, 2010
    • (2010) J Cell Biol , vol.191 , pp. 187-197
    • Johnson, C.P.1    Chapman, E.R.2
  • 76
    • 77952741352 scopus 로고    scopus 로고
    • TRIM72, a novel negative feedback regulator of myogenesis, is transcriptionally activated by the synergism of MyoD (Or myogenin) and MEF2
    • Jung SY, Ko YG. TRIM72, a novel negative feedback regulator of myogenesis, is transcriptionally activated by the synergism of MyoD (or myogenin) and MEF2. Biochem Biophys Res Commun 396: 238-245, 2010
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 238-245
    • Jung, S.Y.1    Ko, Y.G.2
  • 77
    • 84897949693 scopus 로고    scopus 로고
    • Dysferlin at transverse tubules regulates Ca2_ homeostasis in skeletal muscle
    • Kerr JP, Ward CW, Bloch RJ. Dysferlin at transverse tubules regulates Ca2_ homeostasis in skeletal muscle. Front Physiol 5: 89, 2014
    • (2014) Front Physiol , vol.5
    • Kerr, J.P.1    Ward, C.W.2    Bloch, R.J.3
  • 85
  • 89
    • 33751585018 scopus 로고    scopus 로고
    • Annexin2 coating the surface of enlargeosomes is needed for their regulated exocytosis
    • Lorusso A, Covino C, Priori G, Bachi A, Meldolesi J, Chieregatti E. Annexin2 coating the surface of enlargeosomes is needed for their regulated exocytosis. EMBO J 25: 5443-5456, 2006
    • (2006) EMBO J , vol.25 , pp. 5443-5456
    • Lorusso, A.1    Covino, C.2    Priori, G.3    Bachi, A.4    Meldolesi, J.5    Chieregatti, E.6
  • 92
    • 84882662230 scopus 로고    scopus 로고
    • Dysferlin-deficient muscular dystrophy and innate immune activation
    • Mariano A, Henning A, Han R. Dysferlin-deficient muscular dystrophy and innate immune activation. FEBS J 280: 4165-4176, 2013
    • (2013) FEBS J , vol.280 , pp. 4165-4176
    • Mariano, A.1    Henning, A.2    Han, R.3
  • 95
    • 33845951914 scopus 로고    scopus 로고
    • Requirement for annexin A1 in plasma membrane repair
    • McNeil AK, Rescher U, Gerke V, McNeil PL. Requirement for annexin A1 in plasma membrane repair. J Biol Chem 281: 35202-35207, 2006
    • (2006) J Biol Chem , vol.281 , pp. 35202-35207
    • McNeil, A.K.1    Rescher, U.2    Gerke, V.3    McNeil, P.L.4
  • 96
    • 0024602753 scopus 로고
    • Gastrointestinal cell plasma membrane wounding and resealing in vivo
    • McNeil PL, Ito S. Gastrointestinal cell plasma membrane wounding and resealing in vivo. Gastroenterology 96: 1238-1248, 1989
    • (1989) Gastroenterology , vol.96 , pp. 1238-1248
    • McNeil, P.L.1    Ito, S.2
  • 97
    • 0025311957 scopus 로고
    • Molecular traffic through plasma membrane disruptions of cells in vivo
    • McNeil PL, Ito S. Molecular traffic through plasma membrane disruptions of cells in vivo. J Cell Sci 96: 549-556, 1990
    • (1990) J Cell Sci , vol.96 , pp. 549-556
    • McNeil, P.L.1    Ito, S.2
  • 98
    • 0026729383 scopus 로고
    • Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage
    • McNeil PL, Khakee R. Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage. Am J Pathol 140: 1097-1109, 1992
    • (1992) Am J Pathol , vol.140 , pp. 1097-1109
    • McNeil, P.L.1    Khakee, R.2
  • 99
    • 20344402550 scopus 로고    scopus 로고
    • An emergency response team for membrane repair
    • McNeil PL, Kirchhausen T. An emergency response team for membrane repair. Nat Rev Mol Cell Biol 6: 499-505, 2005
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 499-505
    • McNeil, P.L.1    Kirchhausen, T.2
  • 101
    • 34047273570 scopus 로고    scopus 로고
    • Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane
    • Mellgren RL, Zhang W, Miyake K, McNeil PL. Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane. J Biol Chem 282: 2567-2575, 2007
    • (2007) J Biol Chem , vol.282 , pp. 2567-2575
    • Mellgren, R.L.1    Zhang, W.2    Miyake, K.3    McNeil, P.L.4
  • 102
    • 0035939659 scopus 로고    scopus 로고
    • Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity
    • Micheva KD, Holz RW, Smith SJ. Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity. J Cell Biol 154: 355-368, 2001
    • (2001) J Cell Biol , vol.154 , pp. 355-368
    • Micheva, K.D.1    Holz, R.W.2    Smith, S.J.3
  • 103
    • 0028799119 scopus 로고
    • Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal
    • Mikoshiba K, Fukuda M, Moreira JE, Lewis FM, Sugimori M, Niinobe M, Llinás R. Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal. Proc Natl Acad Sci USA 92: 10703-10707, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10703-10707
    • Mikoshiba, K.1    Fukuda, M.2    Moreira, J.E.3    Lewis, F.M.4    Sugimori, M.5    Niinobe, M.6    Llinás, R.7
  • 104
    • 12144291549 scopus 로고    scopus 로고
    • The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/ Rac1-specific guanine nucleotide exchanging factor
    • Mishima W, Suzuki A, Yamaji S, Yoshimi R, Ueda A, Kaneko T, Tanaka J, Miwa Y, Ohno S, Ishigatsubo Y. The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/ Rac1-specific guanine nucleotide exchanging factor. Genes Cells 9: 193-204, 2004
    • (2004) Genes Cells , vol.9 , pp. 193-204
    • Mishima, W.1    Suzuki, A.2    Yamaji, S.3    Yoshimi, R.4    Ueda, A.5    Kaneko, T.6    Tanaka, J.7    Miwa, Y.8    Ohno, S.9    Ishigatsubo, Y.10
  • 105
    • 0141831763 scopus 로고    scopus 로고
    • Mechanical injury and repair of cells
    • Miyake K, McNeil PL. Mechanical injury and repair of cells. Crit Care Med 31: S496-S501, 2003
    • (2003) Crit Care Med , vol.31 , pp. S496-S501
    • Miyake, K.1    McNeil, P.L.2
  • 106
    • 0029585288 scopus 로고
    • Vesicle accumulation and exocytosis at sites of plasma membrane disruption
    • Miyake K, McNeil PL. Vesicle accumulation and exocytosis at sites of plasma membrane disruption. J Cell Biol 131: 1737-1745, 1995
    • (1995) J Cell Biol , vol.131 , pp. 1737-1745
    • Miyake, K.1    McNeil, P.L.2
  • 108
    • 84858230240 scopus 로고    scopus 로고
    • Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein
    • Nabhan JF, Hu R, Oh RS, Cohen SN, Lu Q. Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein. Proc Natl Acad Sci USA 109: 4146-4151, 2012
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4146-4151
    • Nabhan, J.F.1    Hu, R.2    Oh, R.S.3    Cohen, S.N.4    Lu, Q.5
  • 111
    • 84871884783 scopus 로고    scopus 로고
    • Structure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2
    • Ozorowski G, Milton S, Luecke H. Structure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2. Acta Crystallogr D Biol Crystallogr 69: 92-104, 2013
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 92-104
    • Ozorowski, G.1    Milton, S.2    Luecke, H.3
  • 112
    • 0021318476 scopus 로고
    • Lessons for the study of membrane fusion from membrane interactions in phospholipid systems
    • Parsegian VA, Rand RP, Gingell D. Lessons for the study of membrane fusion from membrane interactions in phospholipid systems. Ciba Found Symp 103: 9-27, 1984
    • (1984) Ciba Found Symp , vol.103 , pp. 9-27
    • Parsegian, V.A.1    Rand, R.P.2    Gingell, D.3
  • 113
    • 84899944446 scopus 로고    scopus 로고
    • Amphiphysin 2 (BIN1) in physiology and diseases
    • Prokic I, Cowling BS, Laporte J. Amphiphysin 2 (BIN1) in physiology and diseases. J Mol Med 92: 453-463, 2014
    • (2014) J Mol Med , vol.92 , pp. 453-463
    • Prokic, I.1    Cowling, B.S.2    Laporte, J.3
  • 114
    • 0032876283 scopus 로고    scopus 로고
    • Characteristics of a membrane reservoir buffering membrane tension
    • Raucher D, Sheetz MP. Characteristics of a membrane reservoir buffering membrane tension. Biophys J 77: 1992-2002, 1999
    • (1999) Biophys J , vol.77 , pp. 1992-2002
    • Raucher, D.1    Sheetz, M.P.2
  • 115
    • 0035958557 scopus 로고    scopus 로고
    • Plasma membrane repair is mediated by Ca2_-regulated exocytosis of lysosomes
    • Reddy A, Caler EV, Andrews NW. Plasma membrane repair is mediated by Ca2_-regulated exocytosis of lysosomes. Cell 106: 157-169, 2001
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Rews, N.W.3
  • 117
    • 36349028713 scopus 로고    scopus 로고
    • S100A10/p11: Family, friends and functions
    • Rescher U, Gerke V. S100A10/p11: family, friends and functions. Pflügers Arch 455: 575-582, 2008
    • (2008) Pflügers Arch , vol.455 , pp. 575-582
    • Rescher, U.1    Gerke, V.2
  • 118
    • 81155132217 scopus 로고    scopus 로고
    • The S100A10-annexin A2 complex provides a novel asymmetric platform for membrane repair
    • Rezvanpour A, Santamaria-Kisiel L, Shaw GS. The S100A10-annexin A2 complex provides a novel asymmetric platform for membrane repair. J Biol Chem 286: 40174-40183, 2011
    • (2011) J Biol Chem , vol.286 , pp. 40174-40183
    • Rezvanpour, A.1    Santamaria-Kisiel, L.2    Shaw, G.S.3
  • 120
    • 14844310304 scopus 로고    scopus 로고
    • AlphaPIX associates with calpain 4, the small subunit of calpain, and has a dual role in integrin-mediated cell spreading
    • Rosenberger G, Gal A, Kutsche K. AlphaPIX associates with calpain 4, the small subunit of calpain, and has a dual role in integrin-mediated cell spreading. J Biol Chem 280: 6879-6889, 2005
    • (2005) J Biol Chem , vol.280 , pp. 6879-6889
    • Rosenberger, G.1    Gal, A.2    Kutsche, K.3
  • 123
    • 0029825831 scopus 로고    scopus 로고
    • Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin
    • Schiavo G, Gu QM, Prestwich GD, Söllner TH, Rothman JE. Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin. Proc Natl Acad Sci USA 93: 13327-13332, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13327-13332
    • Schiavo, G.1    Gu, Q.M.2    Prestwich, G.D.3    Söllner, T.H.4    Rothman, J.E.5
  • 124
    • 0029666484 scopus 로고    scopus 로고
    • Zn2_-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene
    • Schissel SL, Schuchman EH, Williams KJ, Tabas I. Zn2_-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene. J Biol Chem 271: 18431-18436, 1996
    • (1996) J Biol Chem , vol.271 , pp. 18431-18436
    • Schissel, S.L.1    Schuchman, E.H.2    Williams, K.J.3    Tabas, I.4
  • 125
    • 12544253372 scopus 로고    scopus 로고
    • Molecular regulation of membrane resealing in 3T3 fibroblasts
    • Shen SS, Tucker WC, Chapman ER, Steinhardt RA. Molecular regulation of membrane resealing in 3T3 fibroblasts. J Biol Chem 280: 1652-1660, 2005
    • (2005) J Biol Chem , vol.280 , pp. 1652-1660
    • Shen, S.S.1    Tucker, W.C.2    Chapman, E.R.3    Steinhardt, R.A.4
  • 126
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt RA, Bi G, Alderton JM. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science 263: 390-393, 1994
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 127
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: A novel Ca2_/phospholipidbinding fold
    • Sutton RB, Davletov BA, Berghuis AM, Südhof TC, Sprang SR. Structure of the first C2 domain of synaptotagmin I: a novel Ca2_/phospholipidbinding fold. Cell 80: 929-938, 1995
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Südhof, T.C.4    Sprang, S.R.5
  • 130
    • 0030801401 scopus 로고    scopus 로고
    • Large plasma membrane disruptions are rapidly resealed by Ca2_-dependent vesicle-vesicle fusion events
    • Terasaki M, Miyake K, McNeil PL. Large plasma membrane disruptions are rapidly resealed by Ca2_-dependent vesicle-vesicle fusion events. J Cell Biol 139: 63-74, 1997
    • (1997) J Cell Biol , vol.139 , pp. 63-74
    • Terasaki, M.1    Miyake, K.2    McNeil, P.L.3
  • 131
    • 0742288022 scopus 로고    scopus 로고
    • Nonmuscle myosin IIA and IIB have distinct functions in the exocytosisdependent process of cell membrane repair
    • Togo T, Steinhardt RA. Nonmuscle myosin IIA and IIB have distinct functions in the exocytosisdependent process of cell membrane repair. Mol Biol Cell 15: 688-695, 2004
    • (2004) Mol Biol Cell , vol.15 , pp. 688-695
    • Togo, T.1    Steinhardt, R.A.2
  • 132
    • 0035094798 scopus 로고    scopus 로고
    • A new dysferlin gene mutation in two Japanese families with limb-girdle muscular dystrophy 2B and Miyoshi myopathy
    • Ueyama H, Kumamoto T, Nagao S, Masuda T, Horinouchi H, Fujimoto S, Tsuda T. A new dysferlin gene mutation in two Japanese families with limb-girdle muscular dystrophy 2B and Miyoshi myopathy. Neuromuscul Disord 11: 139-145, 2001
    • (2001) Neuromuscul Disord , vol.11 , pp. 139-145
    • Ueyama, H.1    Kumamoto, T.2    Nagao, S.3    Masuda, T.4    Horinouchi, H.5    Fujimoto, S.6    Tsuda, T.7
  • 136
    • 37849031506 scopus 로고    scopus 로고
    • Immuno-proteomic approach to excitation: Contraction coupling in skeletal and cardiac muscle: Molecular insights revealed by the mitsugumins
    • Weisleder N, Takeshima H, Ma J. Immuno-proteomic approach to excitation: contraction coupling in skeletal and cardiac muscle: molecular insights revealed by the mitsugumins. Cell Calcium 43: 1-8, 2008
    • (2008) Cell Calcium , vol.43 , pp. 1-8
    • Weisleder, N.1    Takeshima, H.2    Ma, J.3
  • 143
    • 79953836217 scopus 로고    scopus 로고
    • Polymerase transcriptase release factor (PTRF) anchors MG53 protein to cell injury site for initiation of membrane repair
    • Zhu H, Lin P, De G, Choi KH, Takeshima H, Weisleder N, Ma J. Polymerase transcriptase release factor (PTRF) anchors MG53 protein to cell injury site for initiation of membrane repair. J Biol Chem 286: 12820-12824, 2011
    • (2011) J Biol Chem , vol.286 , pp. 12820-12824
    • Zhu, H.1    Lin, P.2    De, G.3    Choi, K.H.4    Takeshima, H.5    Weisleder, N.6    Ma, J.7


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