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Volumn 6, Issue 6, 2005, Pages 499-505

An emergency response team for membrane repair

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; DYSFERLIN; HYBRID PROTEIN;

EID: 20344402550     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1665     Document Type: Review
Times cited : (347)

References (48)
  • 1
    • 0026729383 scopus 로고
    • Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage
    • McNeil, P. L. & 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
  • 2
    • 0029052618 scopus 로고
    • Contraction-induced cell wounding and release of fibroblast growth factor in heart
    • Clarke, M. S., Caldwell, R. W., Chiao, H., Miyake, K. & McNeil, P. L. Contraction-induced cell wounding and release of fibroblast growth factor in heart. Circ. Res. 76, 927-934 (1995).
    • (1995) Circ. Res. , vol.76 , pp. 927-934
    • Clarke, M.S.1    Caldwell, R.W.2    Chiao, H.3    Miyake, K.4    McNeil, P.L.5
  • 3
    • 0032861293 scopus 로고    scopus 로고
    • Apocrine secretion - Fact or artifact?
    • Aumuller, G., Wilhelm, B. & Seitz, J. Apocrine secretion - fact or artifact? Anat. Anz. 181, 437-146 (1999).
    • (1999) Anat. Anz. , vol.181 , pp. 437-146
    • Aumuller, G.1    Wilhelm, B.2    Seitz, J.3
  • 5
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt, R. A., Bi, G. & Alderton, J. M. 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
  • 6
    • 0027058124 scopus 로고
    • On red blood cells, hemolysis and resealed ghosts
    • Hoffman, J. F. On red blood cells, hemolysis and resealed ghosts. Adv. Exp. Med. Biol. 326, 1-15 (1992).
    • (1992) Adv. Exp. Med. Biol. , vol.326 , pp. 1-15
    • Hoffman, J.F.1
  • 7
    • 0037446879 scopus 로고    scopus 로고
    • The endomembrane requirement for cell surface repair
    • McNeil, P. L. Miyake, K. & Vogel, S. S. The endomembrane requirement for cell surface repair. Proc. Natl Acad. Sci. USA 100, 4592-4597 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 4592-4597
    • McNeil, P.L.1    Miyake, K.2    Vogel, S.S.3
  • 8
    • 0024150398 scopus 로고
    • Membrane potential and the cytotoxic Ca cascade of human red blood cells
    • Freedman, J. C. et al. Membrane potential and the cytotoxic Ca cascade of human red blood cells. Soc. Gen. Physiol. Ser 43, 217-231 (1988).
    • (1988) Soc. Gen. Physiol. Ser , vol.43 , pp. 217-231
    • Freedman, J.C.1
  • 9
    • 0033637154 scopus 로고    scopus 로고
    • A decrease in membrane tension precedes successful cell-membrane repair
    • Togo, T., Krasieva, T. B. & Steinhardt, R. A. A decrease in membrane tension precedes successful cell-membrane repair. Mol. Biol. Cell 11, 4339-4346 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4339-4346
    • Togo, T.1    Krasieva, T.B.2    Steinhardt, R.A.3
  • 10
    • 0035344650 scopus 로고    scopus 로고
    • Cell control by membrane-cytoskeleton adhesion
    • Sheetz, M. P. Cell control by membrane-cytoskeleton adhesion. Nature Rev. Mol. Cell Biol. 2, 392-396 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 392-396
    • Sheetz, M.P.1
  • 11
    • 0027408212 scopus 로고
    • Tension-stabilized pores in giant vesicles: Determination of pore size and pore line tension
    • Zhelev, D. V. & Needham, D. Tension-stabilized pores in giant vesicles: determination of pore size and pore line tension. Biochim. Biophys. Acta 1147, 89-104 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1147 , pp. 89-104
    • Zhelev, D.V.1    Needham, D.2
  • 12
    • 0026780702 scopus 로고
    • Syringe loading introduces macromolecules into living mammalian cell cytosol
    • Clarke, M. S. & McNeil, P. L. Syringe loading introduces macromolecules into living mammalian cell cytosol, J. Cell Sci. 102, 535-541 (1992).
    • (1992) J. Cell Sci. , vol.102 , pp. 535-541
    • Clarke, M.S.1    McNeil, P.L.2
  • 14
    • 0035037906 scopus 로고    scopus 로고
    • Cell surface events during resealing visualized by scanning-electron microscopy
    • McNeil, P. L. & Baker, M. M. Cell surface events during resealing visualized by scanning-electron microscopy. Cell Tissue Res. 304, 141-146 (2001).
    • (2001) Cell Tissue Res. , vol.304 , pp. 141-146
    • McNeil, P.L.1    Baker, M.M.2
  • 15
    • 0034130361 scopus 로고    scopus 로고
    • Patching plasma membrane disruptions with cytoplasmic membrane
    • McNeil, P. L., Vogel, S. S., Miyake, K. & Terasaki, M. Patching plasma membrane disruptions with cytoplasmic membrane. J. Cell Sci. 113, 1891-1902 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1891-1902
    • McNeil, P.L.1    Vogel, S.S.2    Miyake, K.3    Terasaki, M.4
  • 16
    • 0029585288 scopus 로고
    • Vesicle accumulation and exocytosis at sites of plasma membrane disruption
    • Miyake, K. & McNeil, P. L. 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
  • 17
    • 0036180245 scopus 로고    scopus 로고
    • Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
    • Wang, L., Seeley, E. S., Wickner, W. & Merz, A. J. Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 108, 357-369 (2002).
    • (2002) Cell , vol.108 , pp. 357-369
    • Wang, L.1    Seeley, E.S.2    Wickner, W.3    Merz, A.J.4
  • 18
    • 0037415612 scopus 로고    scopus 로고
    • Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion
    • Wang, L., Merz, A. J., Colins, K. M. & Wickner, W. Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J. Cell Biol. 160, 365-374 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 365-374
    • Wang, L.1    Merz, A.J.2    Colins, K.M.3    Wickner, W.4
  • 19
    • 0028923312 scopus 로고
    • Lysosome recruitment during host cell invasion by Trypanosoma cruzi
    • Andrews, N. W. Lysosome recruitment during host cell invasion by Trypanosoma cruzi. Trends Cell Biol. 5, 133-137 (1995).
    • (1995) Trends Cell Biol. , vol.5 , pp. 133-137
    • Andrews, N.W.1
  • 20
    • 0035821219 scopus 로고    scopus 로고
    • The exocytosis-regulatory protein synaptotagmin VII mediates cell invasion by Trypanosoma cruzi
    • Caler, E. V., Chakrabarti, S., Fowler, K. T., Rao, S. & Andrews, N. W. The exocytosis-regulatory protein synaptotagmin VII mediates cell invasion by Trypanosoma cruzi. J. Exp. Med. 193, 1097-1104 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 1097-1104
    • Caler, E.V.1    Chakrabarti, S.2    Fowler, K.T.3    Rao, S.4    Andrews, N.W.5
  • 22
    • 0042978564 scopus 로고    scopus 로고
    • Impaired membrane resealing and autoimmune myositis in synaptotagmin VII-deficient mice
    • Chakrabarti, S. et al. Impaired membrane resealing and autoimmune myositis in synaptotagmin VII-deficient mice. J. Cell Biol. 162, 543-549 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 543-549
    • Chakrabarti, S.1
  • 23
    • 19344375822 scopus 로고    scopus 로고
    • Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis
    • Jaiswal, J. K., Chakrabarti, S., Andrews, N. W. & Simon, S. M. Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis. PLoS Biol. 2, E233 (2004).
    • (2004) PLoS Biol. , vol.2
    • Jaiswal, J.K.1    Chakrabarti, S.2    Andrews, N.W.3    Simon, S.M.4
  • 24
    • 9444225430 scopus 로고    scopus 로고
    • 2+-dependent lysosomal exocytosis but not cell resealing
    • 2+-dependent lysosomal exocytosis but not cell resealing. EMBO Rep. 5, 883-888 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 883-888
    • Cerny, J.1
  • 25
    • 0036903036 scopus 로고    scopus 로고
    • Regulated exocytosis: A novel, widely expressed system
    • Borgonovo, B. et al. Regulated exocytosis: a novel, widely expressed system. Nature Cell Biol. 4, 955-962 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 955-962
    • Borgonovo, B.1
  • 26
    • 9444225970 scopus 로고    scopus 로고
    • Enlargeosome, an exocytic vesicle resistant to nonionic detergents, undergoes endocytosis via a nonacidic route
    • Cocucci, E., Racchetti, G., Podini, P., Rupnik, M. & Meldolesi, J. Enlargeosome, an exocytic vesicle resistant to nonionic detergents, undergoes endocytosis via a nonacidic route. Mol. Biol. Cell 15, 5356-5368 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5356-5368
    • Cocucci, E.1    Racchetti, G.2    Podini, P.3    Rupnik, M.4    Meldolesi, J.5
  • 27
    • 0036780223 scopus 로고    scopus 로고
    • Lasker basic medical research award. The machinery and principles of vesicle transport in the cell
    • Rothman, J. E. Lasker basic medical research award. The machinery and principles of vesicle transport in the cell. Nature Med. 8, 1059-1062 (2002).
    • (2002) Nature Med. , vol.8 , pp. 1059-1062
    • Rothman, J.E.1
  • 28
    • 0029609143 scopus 로고
    • Calcium-regulated exocytosis is required for cell membrane resealing
    • Bi, G. Q., Alderton, J. M. & Steinhardt, R. A. 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
  • 30
    • 0034666565 scopus 로고    scopus 로고
    • Axolemmal repair requires proteins that mediate synaptic vesicle fusion
    • Detrait, E. et al. Axolemmal repair requires proteins that mediate synaptic vesicle fusion. J. Neurobiol. 44. 382-391 (2000).
    • (2000) J. Neurobiol. , vol.44 , pp. 382-391
    • Detrait, E.1
  • 31
    • 12544253372 scopus 로고    scopus 로고
    • Molecular regulation of membrane resealing in 3T3 fibroblasts
    • Shen, S. S., Tucker, W. C., Chapman, E. R. & Steinhardt, R. A. Molecular regulation of membrane resealing in 3T3 fibroblasts. J. Biol. Chem. 280, 1652-1660 (2004).
    • (2004) J. Biol. Chem. , vol.280 , pp. 1652-1660
    • Shen, S.S.1    Tucker, W.C.2    Chapman, E.R.3    Steinhardt, R.A.4
  • 32
    • 4143122322 scopus 로고    scopus 로고
    • Resolution of organelle docking and fusion kinetics in a cell-free assay
    • Merz, A. J. & Wickner, W. T. Resolution of organelle docking and fusion kinetics in a cell-free assay. Proc. Natl Acad. Sci. USA 101, 11548-11553 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11548-11553
    • Merz, A.J.1    Wickner, W.T.2
  • 33
    • 0031892178 scopus 로고    scopus 로고
    • Reconstitution of calcium-triggered membrane fusion using 'reserve' granules
    • Chestkov, V. V., Radko, S. P., Cho, M. S., Chrambach, A. & Vogel, S. S. Reconstitution of calcium-triggered membrane fusion using 'reserve' granules. J. Biol. Chem. 273, 2445-2451 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2445-2451
    • Chestkov, V.V.1    Radko, S.P.2    Cho, M.S.3    Chrambach, A.4    Vogel, S.S.5
  • 34
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof, T. C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 22, 645-653 (1995).
    • (1995) Nature , vol.22 , pp. 645-653
    • Sudhof, T.C.1
  • 35
    • 0042858417 scopus 로고    scopus 로고
    • Cell biology of the presynaptic terminal
    • Murthy, V. N. & De Camilli, P. Cell biology of the presynaptic terminal. Annu. Rev. Neurosci. 26, 701-728. (2003).
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 701-728
    • Murthy, V.N.1    De Camilli, P.2
  • 36
    • 17344363640 scopus 로고    scopus 로고
    • A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B
    • Bashir, R. et al. A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B. Nature Genet. 20, 37-42 (1998).
    • (1998) Nature Genet. , vol.20 , pp. 37-42
    • Bashir, R.1
  • 37
    • 17344365600 scopus 로고    scopus 로고
    • Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy
    • Liu, J. et al. Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nature Genet 20, 31-36 (1998).
    • (1998) Nature Genet. , vol.20 , pp. 31-36
    • Liu, J.1
  • 38
    • 0030972880 scopus 로고    scopus 로고
    • A nematode gene required for sperm vesicle fusion
    • Achanzar, W. E. & Ward, S. A nematode gene required for sperm vesicle fusion. J. Cell Sci. 110, 1073-1081 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 1073-1081
    • Achanzar, W.E.1    Ward, S.2
  • 39
    • 0037738510 scopus 로고    scopus 로고
    • Defective membrane repair in dysferlin-deficient muscular dystrophy
    • Bansal, D. et al. Defective membrane repair in dysferlin-deficient muscular dystrophy. Nature 423, 168-172 (2003).
    • (2003) Nature , vol.423 , pp. 168-172
    • Bansal, D.1
  • 40
  • 41
    • 0347379869 scopus 로고    scopus 로고
    • Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing
    • Lennon, N. J. et al. Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing. J. Biol. Chem. 278, 50466-50473 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50466-50473
    • Lennon, N.J.1
  • 42
    • 0033972161 scopus 로고    scopus 로고
    • Myoferlin, a candidate gene and potential modifier of muscular dystrophy
    • Davis, D. B., Delmonte, A. J., Ly, C. T. & McNally, E. M. Myoferlin, a candidate gene and potential modifier of muscular dystrophy. Hum. Mol. Genet. 9, 217-226 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 217-226
    • Davis, D.B.1    Delmonte, A.J.2    Ly, C.T.3    McNally, E.M.4
  • 44
    • 1842556210 scopus 로고    scopus 로고
    • Dysferlin and the plasma membrane repair in muscular dystrophy
    • Bansal, D. & Campbell, K. P. Dysferlin and the plasma membrane repair in muscular dystrophy. Trends Cell Biol. 14, 206-213 (2004).
    • (2004) Trends Cell Biol. , vol.14 , pp. 206-213
    • Bansal, D.1    Campbell, K.P.2
  • 45
    • 1842475284 scopus 로고    scopus 로고
    • Fusion pore dynamics are regulated by synaptotagmin•t-SNARE interactions
    • Bai, J., Wang, C. T., Richards, D. A., Jackson, M. B. & Chapman, E. R. Fusion pore dynamics are regulated by synaptotagmin•t-SNARE interactions. Neuron 41, 929-942 (2004).
    • (2004) Neuron , vol.41 , pp. 929-942
    • Bai, J.1    Wang, C.T.2    Richards, D.A.3    Jackson, M.B.4    Chapman, E.R.5
  • 46
    • 0032947634 scopus 로고    scopus 로고
    • A mutation in OTOF, encoding otoferlin, a FER-1-like protein, causes DFNB9, a nonsyndromic form of deafness
    • Yasunaga, S. et al. A mutation in OTOF, encoding otoferlin, a FER-1-like protein, causes DFNB9, a nonsyndromic form of deafness. Nature Genet. 21, 363-369 (1999).
    • (1999) Nature Genet. , vol.21 , pp. 363-369
    • Yasunaga, S.1
  • 47
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: Repair, prevention, adaptation
    • McNeil, P. L. & Steinhardt, R. Plasma membrane disruption: repair, prevention, adaptation. Annu. Rev. Cell Dev. Biol. 3, 697-731 (2003).
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.3 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.2
  • 48
    • 0033519621 scopus 로고    scopus 로고
    • Wound-induced assembly and closure of an actomyosin purse string in Xenopus oocytes
    • Bernent, W. M., Mandate, C. A. & Kirsch, M. N. Wound-induced assembly and closure of an actomyosin purse string in Xenopus oocytes. Curr. Biol. 9, 579-587 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 579-587
    • Bernent, W.M.1    Mandate, C.A.2    Kirsch, M.N.3


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