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Volumn 141, Issue 6, 1998, Pages 1371-1381

Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; F ACTIN; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 0032526412     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.6.1371     Document Type: Article
Times cited : (168)

References (34)
  • 1
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filamenl turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough, K.R., J. Stryker, N. Pokala, M. Sanders, P. Crews, and D.G. Drubin. 1997. High rates of actin filamenl turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137:399-416.
    • (1997) J. Cell Biol. , vol.137 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 2
    • 0024387979 scopus 로고
    • Reconstitution of protein transport using broken yeast spheroplasts
    • Baker, D., and R. Schekman. 1989. Reconstitution of protein transport using broken yeast spheroplasts. Methods Cell Biol. 31:127-141.
    • (1989) Methods Cell Biol. , vol.31 , pp. 127-141
    • Baker, D.1    Schekman, R.2
  • 3
    • 0031059722 scopus 로고    scopus 로고
    • Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast
    • Berger, K.H., L.F. Sogo, and M.P. Yaffe. 1997. Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast. J. Cell Biol. 136:545-553.
    • (1997) J. Cell Biol. , vol.136 , pp. 545-553
    • Berger, K.H.1    Sogo, L.F.2    Yaffe, M.P.3
  • 4
    • 0018572327 scopus 로고
    • Evidence of microfilament-associated mitochondrial movement
    • Bradley, T.J., and P. Satir. 1979. Evidence of microfilament-associated mitochondrial movement. J. Supramol. Struct. 12:165-175.
    • (1979) J. Supramol. Struct. , vol.12 , pp. 165-175
    • Bradley, T.J.1    Satir, P.2
  • 5
    • 0028129071 scopus 로고
    • MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess, S.M., M. Delannoy, and R.E. Jensen. 1994. MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J. Cell Biol. 126:1375-1391.
    • (1994) J. Cell Biol. , vol.126 , pp. 1375-1391
    • Burgess, S.M.1    Delannoy, M.2    Jensen, R.E.3
  • 6
    • 0027457958 scopus 로고
    • Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro
    • Burkhardt, J.K., J.M. McIlvain, Jr., M.P. Sheetz, and Y. Argon. 1993. Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro. J. Cell Sci. 104:151-162.
    • (1993) J. Cell Sci. , vol.104 , pp. 151-162
    • Burkhardt, J.K.1    McIlvain Jr., J.M.2    Sheetz, M.P.3    Argon, Y.4
  • 7
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J.A. 1987. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105:1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 8
    • 0020479721 scopus 로고
    • Import of proteins into mitochondria. Energy-dependent, two-step processing of the intermembrane space enzyme cytochrome b2 by isolated yeast mitochondria
    • Daum, G., S.M. Gasser, and G. Schatz. 1982. Import of proteins into mitochondria. Energy-dependent, two-step processing of the intermembrane space enzyme cytochrome b2 by isolated yeast mitochondria. J. Biol. Chem. 257: 13075-13080.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13075-13080
    • Daum, G.1    Gasser, S.M.2    Schatz, G.3
  • 9
    • 0027765526 scopus 로고
    • Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • Drubin, D.G., H.D. Jones, and K.F. Wertman. 1993. Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell. 4:1277-1294.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 11
    • 0030951615 scopus 로고    scopus 로고
    • The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton
    • Hermann, G.J., E.J. King, and J.M. Shaw. 1997. The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton. J. Cell Biol. 137:141-153.
    • (1997) J. Cell Biol. , vol.137 , pp. 141-153
    • Hermann, G.J.1    King, E.J.2    Shaw, J.M.3
  • 12
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 13
    • 0026556298 scopus 로고
    • Yeast actin filaments display ATP-dependent sliding movement over surfaces coated with rabbit muscle myosin
    • Kron, S.J., D.G. Drubin, D. Botstein, and J.A. Spudich. 1992. Yeast actin filaments display ATP-dependent sliding movement over surfaces coated with rabbit muscle myosin. Proc. Natl. Acad. Sci. USA. 89:4466-4470.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4466-4470
    • Kron, S.J.1    Drubin, D.G.2    Botstein, D.3    Spudich, J.A.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0028048692 scopus 로고
    • Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity
    • Lazzarino, D.A., I. Boldogh, M.G. Smith, J. Rosand, and L.A. Pon. 1994. Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity. Mol. Biol. Cell. 5:807-818.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 807-818
    • Lazzarino, D.A.1    Boldogh, I.2    Smith, M.G.3    Rosand, J.4    Pon, L.A.5
  • 16
    • 0023803882 scopus 로고
    • Two monoclonal antibodies to actin: One muscle selective and one generally reactive
    • Lessard, J.L. 1988. Two monoclonal antibodies to actin: one muscle selective and one generally reactive. Cell Motil. Cytoskeleton. 10:349-362.
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 349-362
    • Lessard, J.L.1
  • 17
    • 0027286647 scopus 로고
    • Intermediate filament formation by a yeast protein essential for organelle inheritance
    • McConnell, S.J., and M.P. Yaffe. 1993. Intermediate filament formation by a yeast protein essential for organelle inheritance. Science. 260:687-689.
    • (1993) Science , vol.260 , pp. 687-689
    • McConnell, S.J.1    Yaffe, M.P.2
  • 18
    • 0025076787 scopus 로고
    • Temperature-sensitive yeast mutants defective in mitochondrial inheritance
    • McConnell, S.J., L.C. Stewart, A. Talin, and M.P. Yaffe. 1990. Temperature-sensitive yeast mutants defective in mitochondrial inheritance. J. Cell Biol. 111:967-976.
    • (1990) J. Cell Biol. , vol.111 , pp. 967-976
    • McConnell, S.J.1    Stewart, L.C.2    Talin, A.3    Yaffe, M.P.4
  • 19
    • 0025847827 scopus 로고
    • Use of actin filament and microtubule affinity chromatography to identify proteins that bind to the cytoskeleton
    • Miller, K.G., C.M. Field, B.M. Alberts, and D.R. Kellogg. 1991. Use of actin filament and microtubule affinity chromatography to identify proteins that bind to the cytoskeleton. Methods Enzymol. 196:303-319.
    • (1991) Methods Enzymol. , vol.196 , pp. 303-319
    • Miller, K.G.1    Field, C.M.2    Alberts, B.M.3    Kellogg, D.R.4
  • 20
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris, R.L., and P.J. Hollenbeck. 1995. Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J. Cell Biol. 131: 1315-1326.
    • (1995) J. Cell Biol. , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 21
    • 0024829751 scopus 로고
    • Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins
    • Pon, L., T. Moll, D. Vestweber, B. Marshallsay, and G. Schatz. 1989. Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins. J. Cell Biol. 109:2603-2616.
    • (1989) J. Cell Biol. , vol.109 , pp. 2603-2616
    • Pon, L.1    Moll, T.2    Vestweber, D.3    Marshallsay, B.4    Schatz, G.5
  • 22
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 23
    • 0030854830 scopus 로고    scopus 로고
    • Mitochondrial inheritance: Cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae
    • Simon, V.R., S.L. Karmon, and L.A. Pon. 1997. Mitochondrial inheritance: cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae. Cell Motil. Cytoskeleton. 37:199-210.
    • (1997) Cell Motil. Cytoskeleton , vol.37 , pp. 199-210
    • Simon, V.R.1    Karmon, S.L.2    Pon, L.A.3
  • 24
    • 0029078227 scopus 로고
    • Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: Identification of a motor activity on the mitochondrial surface
    • Simon, V.R., T.C. Swayne, and L.A. Pon. 1995. Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: Identification of a motor activity on the mitochondrial surface. J. Cell Biol. 130:345-354.
    • (1995) J. Cell Biol. , vol.130 , pp. 345-354
    • Simon, V.R.1    Swayne, T.C.2    Pon, L.A.3
  • 25
    • 0028157982 scopus 로고
    • The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding
    • Skoufias, D.A., D.G. Cole, K.P. Wedaman, and J.M. Scholey. 1994. The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding. J. Biol. Chem. 269:1477-1485.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1477-1485
    • Skoufias, D.A.1    Cole, D.G.2    Wedaman, K.P.3    Scholey, J.M.4
  • 26
    • 0028799104 scopus 로고
    • Organelle-cytoskeletal interactions: Actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae
    • Smith, M.G., V.R. Simon, H. O'Sullivan, and L.A. Pon. 1995. Organelle-cytoskeletal interactions: actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae. Mol. Biol. Cell. 6:1381-1396.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1381-1396
    • Smith, M.G.1    Simon, V.R.2    O'Sullivan, H.3    Pon, L.A.4
  • 27
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdmq10p, a protein of the mitochondrial outer membrane
    • Sogo, L.F., and M.P. Yaffe. 1994. Regulation of mitochondrial morphology and inheritance by Mdmq10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 126:1361-1373.
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 28
    • 0020698663 scopus 로고
    • Latrunculins: Novel marine toxins that disrupt microfilament organization in cultured cells
    • Spector, I., N.R. Shochet, Y. Kashman, and A. Groweiss. 1983. Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells. Science. 219:493-495.
    • (1983) Science , vol.219 , pp. 493-495
    • Spector, I.1    Shochet, N.R.2    Kashman, Y.3    Groweiss, A.4
  • 29
    • 0029048597 scopus 로고
    • Actin-dependent light-induced translocation of mitochondria and ER cisternae in the photoreceplor cells of the locust Schistocerca gregaria
    • Sturmer, K., O. Baumann, and B. Walz. 1995. Actin-dependent light-induced translocation of mitochondria and ER cisternae in the photoreceplor cells of the locust Schistocerca gregaria. J. Cell Sci. 108:2273-2283.
    • (1995) J. Cell Sci. , vol.108 , pp. 2273-2283
    • Sturmer, K.1    Baumann, O.2    Walz, B.3
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 0026775359 scopus 로고
    • Kinectin, a major kinesin-binding protein on ER
    • Toyoshima, I., H. Yu, E.R. Steuer, and M.P. Sheetz. 1992. Kinectin, a major kinesin-binding protein on ER. J. Cell Biol. 118:1121-1131.
    • (1992) J. Cell Biol. , vol.118 , pp. 1121-1131
    • Toyoshima, I.1    Yu, H.2    Steuer, E.R.3    Sheetz, M.P.4
  • 32
    • 0024818131 scopus 로고
    • The major 45-kDa protein of the yeast mitochondrial outer membrane is not essential for cell growth or mitochondrial function
    • Yaffe, M.P., R.E. Jensen, and E.C. Guido. 1989. The major 45-kDa protein of the yeast mitochondrial outer membrane is not essential for cell growth or mitochondrial function. J. Biol. Chem. 264:21091-21096.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21091-21096
    • Yaffe, M.P.1    Jensen, R.E.2    Guido, E.C.3
  • 33
    • 0029015040 scopus 로고
    • Characterization of kinectin, a kinesin-binding protein: Primary sequence and N-terminal topogenic signal analysis
    • Yu, H., C.V. Nicchitta, J. Kumar, M. Becker, I. Toyoshima, and M.P. Shetz. 1995. Characterization of kinectin, a kinesin-binding protein: primary sequence and N-terminal topogenic signal analysis. Mol. Biol. Cell. 6:171-183.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 171-183
    • Yu, H.1    Nicchitta, C.V.2    Kumar, J.3    Becker, M.4    Toyoshima, I.5    Shetz, M.P.6
  • 34
    • 0031943922 scopus 로고    scopus 로고
    • Functions of the High Mobility Group protein, Abf2p, in mitochondrial DNA segregation, recombination and copy number in Saccharomyces cerevisiae
    • Zelenaya-Troitskaya, O., S.M. Newman, K. Okamoto, P.S. Perlman, , and R.A. Butow. 1997. Functions of the High Mobility Group protein, Abf2p, in mitochondrial DNA segregation, recombination and copy number in Saccharomyces cerevisiae. Genetics. 148:1763-1776.
    • (1997) Genetics , vol.148 , pp. 1763-1776
    • Zelenaya-Troitskaya, O.1    Newman, S.M.2    Okamoto, K.3    Perlman, P.S.4    Butow, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.