메뉴 건너뛰기




Volumn 140, Issue 4, 1998, Pages 873-883

Smy1p, a kinesin-related protein that does not require microtubules

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; KINESIN;

EID: 0032559545     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.4.873     Document Type: Article
Times cited : (64)

References (50)
  • 1
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • Adams, A.E.M., and J.R. Pringle. 1984. Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J. Cell Biol. 98:934-945.
    • (1984) J. Cell Biol. , vol.98 , pp. 934-945
    • Adams, A.E.M.1    Pringle, J.R.2
  • 2
    • 0027954167 scopus 로고
    • The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae
    • Brockerhoff, S.E., R.C. Stevens, and T.N. Davis. 1994. The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae. J. Cell Biol. 124:315-323.
    • (1994) J. Cell Biol. , vol.124 , pp. 315-323
    • Brockerhoff, S.E.1    Stevens, R.C.2    Davis, T.N.3
  • 3
    • 0030750203 scopus 로고    scopus 로고
    • Microtubules orient the mitotic spindle in yeast through dynein-dependent interactions with the cell cortex
    • Carminati, J.L., and T. Stearns. 1997. Microtubules orient the mitotic spindle in yeast through dynein-dependent interactions with the cell cortex. J. Cell Biol. 138:629-641.
    • (1997) J. Cell Biol. , vol.138 , pp. 629-641
    • Carminati, J.L.1    Stearns, T.2
  • 4
    • 0023411053 scopus 로고
    • Structural significance of the GTP-binding domain of ras p21 studied by site-directed mutagenesis
    • Clanton, D.J., Y. Lu, D.G. Blair, and T.Y. Shih. 1987. Structural significance of the GTP-binding domain of ras p21 studied by site-directed mutagenesis. Mol. Cell. Biol. 7:3092-3097.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3092-3097
    • Clanton, D.J.1    Lu, Y.2    Blair, D.G.3    Shih, T.Y.4
  • 5
    • 0030931849 scopus 로고    scopus 로고
    • Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins
    • Cottingham, F.R., and M.A. Hoyt. 1997. Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins. J. Cell Biol. 138:1041-1053.
    • (1997) J. Cell Biol. , vol.138 , pp. 1041-1053
    • Cottingham, F.R.1    Hoyt, M.A.2
  • 6
    • 0030928162 scopus 로고    scopus 로고
    • Kinesin-related KIP3 of Saccharomyces cerevisiae is required for a distinct step in nuclear migration
    • DeZwaan, T.M., E. Ellingson, D. Pellman, and D.M. Roof. 1997. Kinesin-related KIP3 of Saccharomyces cerevisiae is required for a distinct step in nuclear migration. J. Cell Biol. 138:1023-1040.
    • (1997) J. Cell Biol. , vol.138 , pp. 1023-1040
    • DeZwaan, T.M.1    Ellingson, E.2    Pellman, D.3    Roof, D.M.4
  • 7
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath, K.R., G.M. Trimbur, and D.R. Burgess. 1994. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J. Cell Biol. 126:661-675.
    • (1994) J. Cell Biol. , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 8
    • 0027132479 scopus 로고
    • With apologies to Scheherazade: Tails of 1001 kinesin motors
    • Goldstein, L.S.B. 1993. With apologies to Scheherazade: tails of 1001 kinesin motors. Annu. Rev. Genet. 27:319-351.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 319-351
    • Goldstein, L.S.B.1
  • 9
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan, B., R. Bowser, and P. Novick. 1995. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128:1055-1068.
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 10
    • 0028216280 scopus 로고
    • Identification of MYO4, a second class V myosin gene in yeast
    • Haarer, B.K., A. Petzold, S.H. Lillie, and S.S. Brown. 1994. Identification of MYO4, a second class V myosin gene in yeast. J. Cell Sci. 107:1055-1064.
    • (1994) J. Cell Sci. , vol.107 , pp. 1055-1064
    • Haarer, B.K.1    Petzold, A.2    Lillie, S.H.3    Brown, S.S.4
  • 11
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney, D.D. 1994. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl. Acad. Sci. USA. 91: 6865-6869.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 12
    • 0022781503 scopus 로고
    • Yeast/E. coli shuttle vectors with multiple unique restriction sites
    • Hill, J.E., A.M. Meyers, T.J. Koerner, and A. Tzagoloff. 1986. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast. 2:163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Meyers, A.M.2    Koerner, T.J.3    Tzagoloff, A.4
  • 13
    • 0023794908 scopus 로고
    • Diverse effects of β-tubulin mutations on microtubule formation and function
    • Huffaker, T.C., J.H. Thomas, and D. Botstein. 1988. Diverse effects of β-tubulin mutations on microtubule formation and function. J. Cell Biol. 106:1997-2010.
    • (1988) J. Cell Biol. , vol.106 , pp. 1997-2010
    • Huffaker, T.C.1    Thomas, J.H.2    Botstein, D.3
  • 14
    • 0024094565 scopus 로고
    • Functions of microtubules in the Saccharomyces cerevisiae cell cycle
    • Jacobs, C.W., A.E.M. Adams, P.J. Szaniszlo, and J.R. Pringle. 1988. Functions of microtubules in the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 107: 1409-1426.
    • (1988) J. Cell Biol. , vol.107 , pp. 1409-1426
    • Jacobs, C.W.1    Adams, A.E.M.2    Szaniszlo, P.J.3    Pringle, J.R.4
  • 15
    • 0018955106 scopus 로고
    • Ribosomal precursor RNA metabolism and cell division in the yeast Saccharomyces cerevisiae
    • Johnston, G.C., and R.A. Singer. 1980. Ribosomal precursor RNA metabolism and cell division in the yeast Saccharomyces cerevisiae. Molec. Gen. Genet. 178:357-360.
    • (1980) Molec. Gen. Genet. , vol.178 , pp. 357-360
    • Johnston, G.C.1    Singer, R.A.2
  • 16
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston, G.C., J.A. Prendergast, and R.A. Singer. 1991. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113:539-551.
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 17
    • 0021369651 scopus 로고
    • Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces
    • Kilmartin, J.V., and A.E.M. Adams. 1984. Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J. Cell Biol. 98: 922-933.
    • (1984) J. Cell Biol. , vol.98 , pp. 922-933
    • Kilmartin, J.V.1    Adams, A.E.M.2
  • 18
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull, F.J., E.P. Sablin, R. Lau, R.J. Fletterick, and R.D. Vale. 1996. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature. 380:550-555.
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 19
    • 0028942256 scopus 로고
    • Actin- and microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford, G.M. 1995. Actin-and microtubule-dependent organelle motors: interrelationships between the two motility systems. Cnrr. Opin. Cell Biol. 7:82-88.
    • (1995) Cnrr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 20
    • 0019187844 scopus 로고
    • Reserve carbohydrate metabolism in Saccharomyces cerevisiae: Responses to nutrient limitation
    • Lillie, S.H., and J.R. Pringle. 1980. Reserve carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation. J. Bacteriol. 143: 1384-1394.
    • (1980) J. Bacteriol. , vol.143 , pp. 1384-1394
    • Lillie, S.H.1    Pringle, J.R.2
  • 21
    • 0026539415 scopus 로고
    • Suppression of a myosin defect by a kinesin-related gene
    • Lillie, S.H., and S.S. Brown. 1992. Suppression of a myosin defect by a kinesin-related gene. Nature. 356:358-361.
    • (1992) Nature , vol.356 , pp. 358-361
    • Lillie, S.H.1    Brown, S.S.2
  • 22
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie, S.H., and S.S. Brown. 1994. Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae. J. Cell Biol. 125:825-842.
    • (1994) J. Cell Biol. , vol.125 , pp. 825-842
    • Lillie, S.H.1    Brown, S.S.2
  • 23
    • 0026770695 scopus 로고
    • Characterization of TPM1 disrupted yeast cells indicates an involvement of tropomyosin in directed vesicular transport
    • Liu, H., and A. Bretscher. 1992. Characterization of TPM1 disrupted yeast cells indicates an involvement of tropomyosin in directed vesicular transport. J. Cell Biol. 118:285-299.
    • (1992) J. Cell Biol. , vol.118 , pp. 285-299
    • Liu, H.1    Bretscher, A.2
  • 24
    • 0023988582 scopus 로고
    • Site-directed mutagenesis of a nucleotide-binding domain in HSV-1 thymidine kinase: Effects on catalytic activity
    • Liu, Q.Y., and W.C. Summers. 1988. Site-directed mutagenesis of a nucleotide-binding domain in HSV-1 thymidine kinase: effects on catalytic activity. Virology. 163:638-642.
    • (1988) Virology , vol.163 , pp. 638-642
    • Liu, Q.Y.1    Summers, W.C.2
  • 25
    • 0027293707 scopus 로고
    • Mutagenesis of the P-loop motif in the ATP binding site of the RecA protein from Escherichia coli
    • Logan, K.M., and K.L. Knight. 1993. Mutagenesis of the P-loop motif in the ATP binding site of the RecA protein from Escherichia coli. J. Mol. Biol. 232:1048-1059.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1048-1059
    • Logan, K.M.1    Knight, K.L.2
  • 26
    • 0025309665 scopus 로고
    • KAR3, a kinesin-related gene required for yeast nuclear fusion
    • Meluh, P.B., and M.D. Rose. 1990. KAR3, a kinesin-related gene required for yeast nuclear fusion. Cell. 60:1029-1041.
    • (1990) Cell , vol.60 , pp. 1029-1041
    • Meluh, P.B.1    Rose, M.D.2
  • 27
    • 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
  • 29
    • 0025336325 scopus 로고
    • Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain
    • Nair, J., H. Muller, M. Peterson, and P. Novick. 1990. Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain. J. Cell Biol. 110:1897-1909.
    • (1990) J. Cell Biol. , vol.110 , pp. 1897-1909
    • Nair, J.1    Muller, H.2    Peterson, M.3    Novick, P.4
  • 30
    • 0021906692 scopus 로고
    • Phenotypic analysis of temperature-sensitive yeast actin mutants
    • Novick, P., and D. Botstein. 1985. Phenotypic analysis of temperature-sensitive yeast actin mutants. Cell. 40:405-116.
    • (1985) Cell , vol.40 , pp. 405-1116
    • Novick, P.1    Botstein, D.2
  • 31
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35Å 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 1.35Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:2351-2359.
    • (1990) EMBO 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
  • 32
    • 0023147386 scopus 로고
    • Effect of cell cycle position on thermotolerance in Saccharomyces cerevisiae
    • Plesset, J., J.R. Ludwig, B.S. Cox, and C.S. McLaughlin. 1987. Effect of cell cycle position on thermotolerance in Saccharomyces cerevisiae. J. Bacteriol. 169:779-784.
    • (1987) J. Bacteriol. , vol.169 , pp. 779-784
    • Plesset, J.1    Ludwig, J.R.2    Cox, B.S.3    McLaughlin, C.S.4
  • 33
    • 0030921711 scopus 로고    scopus 로고
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex. J. Cell Biol. 137:1589-1601.
    • (1997) J. Cell Biol. , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 34
    • 0027056183 scopus 로고
    • Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy
    • Preuss, D., J. Mulholland, A. Franzusoff, N. Segev, and D. Botstein. 1992. Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy. Mol. Biol. Cell. 3:789-803.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 789-803
    • Preuss, D.1    Mulholland, J.2    Franzusoff, A.3    Segev, N.4    Botstein, D.5
  • 36
    • 0029878485 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the kinesin-related motor ncd
    • Sablin, E.P., F.J. Kull, R. Cooke, R.D. Vale, and R.J. Fletterick. 1996. Crystal structure of the motor domain of the kinesin-related motor ncd. Nature. 380: 555-559.
    • (1996) Nature , vol.380 , pp. 555-559
    • Sablin, E.P.1    Kull, F.J.2    Cooke, R.3    Vale, R.D.4    Fletterick, R.J.5
  • 37
    • 0023662281 scopus 로고
    • A ras-like protein is required for a post-Golgi event in yeast secretion
    • Salminen, A., and P.J. Novick. 1987. A ras-like protein is required for a post-Golgi event in yeast secretion. Cell. 49:527-538.
    • (1987) Cell , vol.49 , pp. 527-538
    • Salminen, A.1    Novick, P.J.2
  • 39
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., P.R. Sibbald, and A. Wittinghofer. 1990. The P-loop - a common motif in ATP-and GTP-binding proteins. Trends Biochem. Sci. 15:430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 42
    • 0030754171 scopus 로고    scopus 로고
    • Costal2, a novel kinesin-related protein in the hedgehog signaling pathway
    • Sisson, J.C., K.S. Ho, K. Suyama, and M.P. Scott. 1997. Costal2, a novel kinesin-related protein in the hedgehog signaling pathway. Cell 90:235-245.
    • (1997) Cell , vol.90 , pp. 235-245
    • Sisson, J.C.1    Ho, K.S.2    Suyama, K.3    Scott, M.P.4
  • 43
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • Smith, C.A., and I. Rayment. 1996. Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys. J. 70:1590-1602.
    • (1996) Biophys. J. , vol.70 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 44
    • 0024024370 scopus 로고
    • Unlinked noncomplementation: Isolation of new conditional-lethal mutations in each of the lubulin genes of Saccharomyces cerevisiae
    • Stearns, T., and D. Botstein. 1988. Unlinked noncomplementation: isolation of new conditional-lethal mutations in each of the lubulin genes of Saccharomyces cerevisiae. Genetics. 119:249-260.
    • (1988) Genetics , vol.119 , pp. 249-260
    • Stearns, T.1    Botstein, D.2
  • 45
    • 0029045404 scopus 로고
    • Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae
    • TerBush, D.R., and P. Novick. 1995. Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae. J. Cell Biol. 130:299-312.
    • (1995) J. Cell Biol. , vol.130 , pp. 299-312
    • Terbush, D.R.1    Novick, P.2
  • 46
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush, D.R., T. Maurice, D. Roth, and P. Novick. 1996. The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15:6483-6494.
    • (1996) EMBO J. , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 47
    • 0022408888 scopus 로고
    • Isolation and characterization of mutations in the β-tubulin gene of Saccharomyces cerevisiae
    • Thomas, J.H., N.F. Neff, and D. Botstein. 1985. Isolation and characterization of mutations in the β-tubulin gene of Saccharomyces cerevisiae. Genetics. 111:715-734.
    • (1985) Genetics , vol.111 , pp. 715-734
    • Thomas, J.H.1    Neff, N.F.2    Botstein, D.3
  • 48
    • 0030930514 scopus 로고    scopus 로고
    • Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles
    • Walch-Solimena, C., R.N. Collins, and P.J. Novick. 1997. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137:1495-1509.
    • (1997) J. Cell Biol. , vol.137 , pp. 1495-1509
    • Walch-Solimena, C.1    Collins, R.N.2    Novick, P.J.3
  • 50
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
    • Yang, L.T., R.A. Laymon, and L.S.B. Goldstein. 1989. A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses. Cell. 56:879-889.
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, L.T.1    Laymon, R.A.2    Goldstein, L.S.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.