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Volumn 143, Issue 2, 1998, Pages 333-349

The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast

Author keywords

Dynamin; GTPase; Membrane morphology; Mitochondria; S. cerevisiae

Indexed keywords

DYNAMIN; GUANOSINE TRIPHOSPHATASE;

EID: 0032547797     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.2.333     Document Type: Article
Times cited : (349)

References (72)
  • 1
    • 0024294392 scopus 로고
    • Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain
    • Adari, H., D.R. Lowy, B.M. Willumsen, C.J. Der, and F. McCormick. 1988. Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. Science. 240:518-521.
    • (1988) Science , vol.240 , pp. 518-521
    • Adari, H.1    Lowy, D.R.2    Willumsen, B.M.3    Der, C.J.4    McCormick, F.5
  • 2
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst, M., T.K. Sato, L.M. Banta, and S.D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO (Eur. Mol. Biol. Organ.) J. 16:1820-1831.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 3
    • 0017877645 scopus 로고
    • Mitochondrial framework (reticulum mitochondriale) in rat diaphragm muscle
    • Bakeeva, L.E., Y.S. Chentsov, and V.P. Skulachev. 1978. Mitochondrial framework (reticulum mitochondriale) in rat diaphragm muscle. Biochim. Biophys. Acta. 501:349-369.
    • (1978) Biochim. Biophys. Acta , vol.501 , pp. 349-369
    • Bakeeva, L.E.1    Chentsov, Y.S.2    Skulachev, V.P.3
  • 4
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast
    • Benedetti, H., S. Raths, F. Crausaz, and H. Riezman. 1994. The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Mol. Biol. Cell. 5:1023-1037.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 1023-1037
    • Benedetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 5
    • 0025036216 scopus 로고
    • Behavior of mitochondria in the living cell
    • Bereiter-Hahn, J. 1990. Behavior of mitochondria in the living cell. Int. Rev. Cytol. 122:1-63.
    • (1990) Int. Rev. Cytol. , vol.122 , pp. 1-63
    • Bereiter-Hahn, J.1
  • 6
    • 0028047262 scopus 로고
    • Dynamics of mitochondria in living cells: Shape changes, dislocations, fusion, and fission of mitochondria
    • Bereiter-Hahn, J., and M. Voth. 1994. Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria. Microsc. Res. Tech. 27:198-219.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 198-219
    • Bereiter-Hahn, J.1    Voth, M.2
  • 7
    • 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
  • 8
    • 0032526412 scopus 로고    scopus 로고
    • Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p
    • Boidogh, I., Vojtov, N., Karmon, S., and L.A. Pon. 1998. Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p. J. Cell Biol. 141:1371-1381.
    • (1998) J. Cell Biol. , vol.141 , pp. 1371-1381
    • Boidogh, I.1    Vojtov, N.2    Karmon, S.3    Pon, L.A.4
  • 9
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., D.A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 10
    • 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
  • 11
    • 0024280502 scopus 로고
    • The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product
    • Cales, C., J.F. Hancock, C.J. Marshall, and A. Hall. 1988. The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product. Nature. 332:548-551.
    • (1988) Nature , vol.332 , pp. 548-551
    • Cales, C.1    Hancock, J.F.2    Marshall, C.J.3    Hall, A.4
  • 13
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke, H., T. Baba, D.E. Warnock, and S.L. Sehmid. 1994. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127:915-934.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Sehmid, S.L.4
  • 14
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke, H., T. Baba, A.M. van der Bliek, and S.L. Sehmid. 1995. Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J. Cell Biol. 131:69-80.
    • (1995) J. Cell Biol. , vol.131 , pp. 69-80
    • Damke, H.1    Baba, T.2    Van Der Bliek, A.M.3    Sehmid, S.L.4
  • 15
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria
    • Daum, G., P.C. Bohni, and G. Schatz. 1982. Import of proteins into mitochondria. J. Biol. Chem. 257:13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 17
    • 0023715225 scopus 로고
    • Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP
    • Feig, L.A., and G.M. Cooper. 1988. Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP. Mol. Cell. Biol. 8:3235-3243.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3235-3243
    • Feig, L.A.1    Cooper, G.M.2
  • 18
    • 0001926223 scopus 로고
    • Spermatogenesis
    • M. Bate and A. Martinez-Arias, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Fuller, M.T. 1993. Spermatogenesis. In The Development of Drosophila melanogaster. M. Bate and A. Martinez-Arias, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 71-147.
    • (1993) The Development of Drosophila melanogaster , pp. 71-147
    • Fuller, M.T.1
  • 19
    • 0029082226 scopus 로고
    • DNM1, a dynamin-related gene, participates in endosomal trafficking in yeast
    • Gammie, A.E., L.J. Kurihara, R.B. Vallee, and M.D. Rose. 1995. DNM1, a dynamin-related gene, participates in endosomal trafficking in yeast. J. Cell Biol. 130:553-566.
    • (1995) J. Cell Biol. , vol.130 , pp. 553-566
    • Gammie, A.E.1    Kurihara, L.J.2    Vallee, R.B.3    Rose, M.D.4
  • 20
    • 0031079689 scopus 로고    scopus 로고
    • Dynamics of phragmoplastin in living cells during cell plate formation and uncoupling of cell elongation from the plane of cell division
    • Gu, X., and D.P.S. Verma. 1997. Dynamics of phragmoplastin in living cells during cell plate formation and uncoupling of cell elongation from the plane of cell division. Plant Cell. 9:157-169.
    • (1997) Plant Cell. , vol.9 , pp. 157-169
    • Gu, X.1    Verma, D.P.S.2
  • 21
    • 0027172432 scopus 로고
    • Normal mitochondrial structure and genome maintenance in yeast requires the dynamin-like product of the MGM1 gene
    • Guan, K., L. Farh, T.K. Marshall, and R.J. Deschenes. 1993. Normal mitochondrial structure and genome maintenance in yeast requires the dynamin-like product of the MGM1 gene. Curr. Genet. 24:141-148.
    • (1993) Curr. Genet. , vol.24 , pp. 141-148
    • Guan, K.1    Farh, L.2    Marshall, T.K.3    Deschenes, R.J.4
  • 23
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley, J.R., and M.A. McNiven. 1996. Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133:761-775.
    • (1996) J. Cell Biol. , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 25
    • 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
  • 28
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw, J.E., and S.L. Schmid. 1995. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature. 374:190-192.
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 29
    • 0031799717 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p
    • Imoto, M., I. Tachibana, and R. Urrutia. 1998. Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p. J. Cell Sci. 111:1341-1349.
    • (1998) J. Cell Sci. , vol.111 , pp. 1341-1349
    • Imoto, M.1    Tachibana, I.2    Urrutia, R.3
  • 30
    • 0026544936 scopus 로고
    • Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin
    • Jones, B.A., and W.L. Fangman. 1992. Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin. Genes Dev. 6:380-389.
    • (1992) Genes Dev. , vol.6 , pp. 380-389
    • Jones, B.A.1    Fangman, W.L.2
  • 31
    • 0032559342 scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones, S.M., K.E. Howell, J.R. Henley, H. Cao, and M.A. McNiven. 1988. Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science. 279:573-577.
    • (1988) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 32
    • 0031985126 scopus 로고    scopus 로고
    • Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl terminal domain in mammalian cells
    • Kamimoto, T., Y. Nagai, H. Onogi, Y. Muro, T. Wakabayashi, and M. Hagiwara. 1998. Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl terminal domain in mammalian cells. J. Biol. Chem. 273:1044-1051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1044-1051
    • Kamimoto, T.1    Nagai, Y.2    Onogi, H.3    Muro, Y.4    Wakabayashi, T.5    Hagiwara, M.6
  • 33
    • 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
  • 34
    • 0028805690 scopus 로고
    • Dynamin and endocytosis
    • Liu, J.P., and P.J. Robinson. 1995. Dynamin and endocytosis. Endocrine Rev. 16:590-607.
    • (1995) Endocrine Rev. , vol.16 , pp. 590-607
    • Liu, J.P.1    Robinson, P.J.2
  • 35
    • 0026690840 scopus 로고
    • Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein
    • McConnell, S.J., and M.P. Yaffe. 1992. Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein. J. Cell Biol. 118:385-395.
    • (1992) J. Cell Biol. , vol.118 , pp. 385-395
    • McConnell, S.J.1    Yaffe, M.P.2
  • 36
    • 0027997975 scopus 로고
    • Endocytosis is required for the growth of vacuolar H+-ATPase defective yeast: Identification of six new END genes
    • Munn, A.L., and H. Riezman. 1994. Endocytosis is required for the growth of vacuolar H+-ATPase defective yeast: identification of six new END genes. J. Cell Biol. 127:373-386.
    • (1994) J. Cell Biol. , vol.127 , pp. 373-386
    • Munn, A.L.1    Riezman, H.2
  • 37
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 angstrom resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E.F., U. Krengel, G.A. Petsko, R.S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 angstrom resolution: implications for the mechanism of GTP hydrolysis. EMBO (Eur. Mol. Biol. Organ.) J. 9:2351-2359.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 39
    • 0018332644 scopus 로고
    • Reversible alterations in the neuromuscular junctions of Drosophila melanogaster bearing a temperature-sensitive mutation, shibire
    • Poodry, C.A., and L. Edgar. 1979. Reversible alterations in the neuromuscular junctions of Drosophila melanogaster bearing a temperature-sensitive mutation, shibire. J. Cell Biol. 81:520-527.
    • (1979) J. Cell Biol. , vol.81 , pp. 520-527
    • Poodry, C.A.1    Edgar, L.2
  • 41
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in the receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., J. Rohrer, F. Crausaz, and H. Riezman. 1993. end3 and end4: two mutants defective in the receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120:55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 42
    • 0025932536 scopus 로고
    • A putative zinc finger protein, Saccharomyces cerevisiae Vps18p, affects late Golgi functions required for vacuolar protein sorting and efficient α-factor prohormone maturation
    • Robinson, J.S., T.R. Graham, and S.D. Emr. 1991. A putative zinc finger protein, Saccharomyces cerevisiae Vps18p, affects late Golgi functions required for vacuolar protein sorting and efficient α-factor prohormone maturation. Mol. Cell Biol. 11:5813-5824.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5813-5824
    • Robinson, J.S.1    Graham, T.R.2    Emr, S.D.3
  • 43
    • 0031921170 scopus 로고    scopus 로고
    • Mitochondrial inheritance is delayed in Saccharomyces cerevisiae cells lacking the serine/threonine phosphatase
    • Roeder, A.D., G.J. Hermann, B.R. Keegan, S.A. Thatcher, and J.M. Shaw. 1998. Mitochondrial inheritance is delayed in Saccharomyces cerevisiae cells lacking the serine/threonine phosphatase. PTC1. Mol. Biol. Cell. 9:917-930.
    • (1998) PTC1. Mol. Biol. Cell. , vol.9 , pp. 917-930
    • Roeder, A.D.1    Hermann, G.J.2    Keegan, B.R.3    Thatcher, S.A.4    Shaw, J.M.5
  • 44
    • 0029839347 scopus 로고    scopus 로고
    • Vacuole partitioning during meiotic division in yeast
    • Roeder, A.D., and J.M. Shaw. 1996. Vacuole partitioning during meiotic division in yeast. Genetics. 144:445-458.
    • (1996) Genetics , vol.144 , pp. 445-458
    • Roeder, A.D.1    Shaw, J.M.2
  • 45
    • 0025376380 scopus 로고
    • A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting
    • Rothman, J.H., C.K. Raymond, T. Gilbert, P.J. O'Hara, and T.H. Stevens. 1990. A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting. Cell. 61: 1063-1074.
    • (1990) Cell , vol.61 , pp. 1063-1074
    • Rothman, J.H.1    Raymond, C.K.2    Gilbert, T.3    O'Hara, P.J.4    Stevens, T.H.5
  • 46
    • 0025335298 scopus 로고
    • Propagation and expression of cloned genes in yeast: 2 micron circle based vectors
    • Rose, A.B., and J.R. Broach. 1990. Propagation and expression of cloned genes in yeast: 2 micron circle based vectors. Methods Enzymol. 185:234-279.
    • (1990) Methods Enzymol. , vol.185 , pp. 234-279
    • Rose, A.B.1    Broach, J.R.2
  • 47
    • 0023545322 scopus 로고
    • A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
    • Rose, M.D., P. Novick, J.H. Thomas, D. Botstein, and G.R. Fink. 1987. A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene (Amst.). 60:237-243.
    • (1987) Gene (Amst.) , vol.60 , pp. 237-243
    • Rose, M.D.1    Novick, P.2    Thomas, J.H.3    Botstein, D.4    Fink, G.R.5
  • 48
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S.L. 1997. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66:511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 49
    • 0028841139 scopus 로고
    • Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae
    • Schneider, B.L., W. Seufert, B. Steiner, Q.H. Yang, and A.B. Futcher. 1995. Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae. Yeast. 11:1265-1274.
    • (1995) Yeast , vol.11 , pp. 1265-1274
    • Schneider, B.L.1    Seufert, W.2    Steiner, B.3    Yang, Q.H.4    Futcher, A.B.5
  • 51
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C.E., and P. Walter. 1996. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO (Eur. Mol. Biol. Organ.) J. 15:3028-3039.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 53
    • 0030817913 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p
    • Shin, H.-W., C. Shinotsuka, S. Torii, K. Murakami, and K. Nakayama. 1997. Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p. J. Biochem. 122: 525-530.
    • (1997) J. Biochem. , vol.122 , pp. 525-530
    • Shin, H.-W.1    Shinotsuka, C.2    Torii, S.3    Murakami, K.4    Nakayama, K.5
  • 54
    • 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
  • 55
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and Inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L.F., and M.P. Yaffe. 1994. Regulation of mitochondrial morphology and Inheritance by Mdm10p, 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
  • 56
    • 0031408332 scopus 로고    scopus 로고
    • The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole
    • Stepp, J.D., K. Huang, and S.K. Lemmon. 1997. The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole. J. Cell Biol. 139:1761-1774.
    • (1997) J. Cell Biol. , vol.139 , pp. 1761-1774
    • Stepp, J.D.1    Huang, K.2    Lemmon, S.K.3
  • 57
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer, S.M., and J.E. Hinshaw. 1998. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell. 93:1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 58
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTPγS in nerve terminals
    • Takei, K., P.S. McPherson, S.L. Schmid, and P. De Camilli. 1995. Tubular membrane invaginations coated by dynamin rings are induced by GTPγS in nerve terminals. Nature. 374:186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 59
    • 0031026631 scopus 로고    scopus 로고
    • The dynamins: Redundant or distinct functions for an expanding family of related GTPases?
    • Urrutia, R., J.R. Henley, T. Cook, and M.A. McNiven. 1997. The dynamins: redundant or distinct functions for an expanding family of related GTPases? Proc. Natl. Acad. Sci. USA. 94:377-384.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 377-384
    • Urrutia, R.1    Henley, J.R.2    Cook, T.3    McNiven, M.A.4
  • 60
    • 0025810110 scopus 로고
    • Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic
    • van der Bliek, A.M., and E.M. Meyerowitz. 1991. Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic. Nature. 351:411-414.
    • (1991) Nature , vol.351 , pp. 411-414
    • Van Der Bliek, A.M.1    Meyerowitz, E.M.2
  • 62
    • 0026471712 scopus 로고
    • The VPS1 protein, a homolog of dynamin required for vacuolar protein sorting in Saccharomyces cerevisiae
    • Vater, C.A., C.K. Raymond, K. Ekena, I. Howald-Stevenson, and T.H. Stevens. 1992. The VPS1 protein, a homolog of dynamin required for vacuolar protein sorting in Saccharomyces cerevisiae. J. Cell Biol. 119:773-786.
    • (1992) J. Cell Biol. , vol.119 , pp. 773-786
    • Vater, C.A.1    Raymond, C.K.2    Ekena, K.3    Howald-Stevenson, I.4    Stevens, T.H.5
  • 63
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A., and S.D. Emr. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128:779-792.
    • (1995) J. Cell Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 64
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Voitek, A.B., S.M. Hollenberg, and J.A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell. 74:205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Voitek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 65
    • 0032079666 scopus 로고    scopus 로고
    • A dileucine-like sorting signal directs transport into an AP-3-dependent, clathrin-independent pathway to the yeast vacuole
    • Vowels, J.J., and G.S. Payne. 1998. A dileucine-like sorting signal directs transport into an AP-3-dependent, clathrin-independent pathway to the yeast vacuole. EMBO (Eur. Mol. Biol. Organ.) J. 17:2482-2493.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 2482-2493
    • Vowels, J.J.1    Payne, G.S.2
  • 67
    • 0029787352 scopus 로고    scopus 로고
    • Dynamin self-assembly stimulates its GTPase activity
    • Warnock, D.E., J.E. Hinshaw, and S.L. Schmid. 1996. Dynamin self-assembly stimulates its GTPase activity. J. Biol. Chem. 271:22310-22314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22310-22314
    • Warnock, D.E.1    Hinshaw, J.E.2    Schmid, S.L.3
  • 68
    • 0030298146 scopus 로고    scopus 로고
    • Dynamin GTPase, a force generating molecular switch
    • Warnock, D.E., and S.L. Schmid. 1996. Dynamin GTPase, a force generating molecular switch. Bioessays. 18:885-893.
    • (1996) Bioessays , vol.18 , pp. 885-893
    • Warnock, D.E.1    Schmid, S.L.2
  • 69
    • 12644263389 scopus 로고    scopus 로고
    • A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15
    • Wendland, B., M.J. McCaffery, Q. Xiao, and S.D. Emr. 1996. A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. J. Cell Biol. 135:1485-1500.
    • (1996) J. Cell Biol. , vol.135 , pp. 1485-1500
    • Wendland, B.1    McCaffery, M.J.2    Xiao, Q.3    Emr, S.D.4
  • 70
    • 0028794516 scopus 로고
    • Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S228C
    • Winston, F., C. Dollard, and S.L. Ricupero-Hovasse. 1995. Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S228C. Yeast. 11:53-55.
    • (1995) Yeast , vol.11 , pp. 53-55
    • Winston, F.1    Dollard, C.2    Ricupero-Hovasse, S.L.3
  • 71
    • 0032559599 scopus 로고    scopus 로고
    • A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells
    • Yoon, Y., K.R. Pitts, S. Dahan, and M.A. McNiven. 1998. A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. J. Cell Biol. 140:779-793.
    • (1998) J. Cell Biol. , vol.140 , pp. 779-793
    • Yoon, Y.1    Pitts, K.R.2    Dahan, S.3    McNiven, M.A.4
  • 72
    • 0029009125 scopus 로고
    • Isolation and biochemical characterization of organelles from the yeast. Saccharomyces cerevisiae
    • Zinser E., and G. Daum. 1995. Isolation and biochemical characterization of organelles from the yeast. Saccharomyces cerevisiae. Yeast. 11:493-536.
    • (1995) Yeast , vol.11 , pp. 493-536
    • Zinser, E.1    Daum, G.2


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