메뉴 건너뛰기




Volumn 143, Issue 7, 1998, Pages 1931-1945

Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast

Author keywords

Actin; MYO2; Polarity; SEC4; Tropomyosin

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATASE; MYOSIN; TROPOMYOSIN;

EID: 0032576569     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.7.1931     Document Type: Article
Times cited : (288)

References (39)
  • 1
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud-growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • Adams, A., and J. 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.1    Pringle, J.2
  • 2
    • 0025294640 scopus 로고
    • CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae
    • Adams, A., D. Johnston, R. Longnecker, B. Sloat, and J. Pringle. 1990. CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. J. Cell Biol. 111:131-142.
    • (1990) J. Cell Biol. , vol.111 , pp. 131-142
    • Adams, A.1    Johnston, D.2    Longnecker, R.3    Sloat, B.4    Pringle, J.5
  • 3
    • 0025983823 scopus 로고
    • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo
    • Adams, A., D. Botstein, and D. Drubin. 1991. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature. 354:404-408.
    • (1991) Nature , vol.354 , pp. 404-408
    • Adams, A.1    Botstein, D.2    Drubin, D.3
  • 4
    • 0025344531 scopus 로고
    • Disruption of the actin cytoskeleton in yeast capping protein mutants
    • Amatruda, J., J. Cannon, K. Tatchell, C. Hug, and J. Cooper. 1990. Disruption of the actin cytoskeleton in yeast capping protein mutants. Nature. 344:352-354.
    • (1990) Nature , vol.344 , pp. 352-354
    • Amatruda, J.1    Cannon, J.2    Tatchell, K.3    Hug, C.4    Cooper, J.5
  • 5
    • 0026482118 scopus 로고
    • Effects of null mutations and overexpression of capping protein on morphogenesis, actin distribution, and polarized secretion in yeast
    • Amatruda, J., D. Gattermeir, T. Karpova, and J. Cooper. 1992. Effects of null mutations and overexpression of capping protein on morphogenesis, actin distribution, and polarized secretion in yeast. J. Cell Biol. 119:1151-1162.
    • (1992) J. Cell Biol. , vol.119 , pp. 1151-1162
    • Amatruda, J.1    Gattermeir, D.2    Karpova, T.3    Cooper, J.4
  • 6
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough, K., J. Stryker, N. Pokala, M. Sanders, P. Crews, and D. Drubin. 1997. High rates of actin 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.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.6
  • 7
    • 0026438291 scopus 로고
    • A new tropomyosin essential for cytokinesis in the fission yeast 5. pombe
    • Balasubramanian, M., D. Helfman, and S. Hemmingsen. 1992. A new tropomyosin essential for cytokinesis in the fission yeast 5. pombe. Nature. 360:84-87.
    • (1992) Nature , vol.360 , pp. 84-87
    • Balasubramanian, M.1    Helfman, D.2    Hemmingsen, S.3
  • 8
    • 0025313449 scopus 로고
    • Isolation, characterization, and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects
    • Ballou, C. 1990. Isolation, characterization, and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects. Methods Enzymol. 185:440-470.
    • (1990) Methods Enzymol. , vol.185 , pp. 440-470
    • Ballou, C.1
  • 9
    • 0032494082 scopus 로고    scopus 로고
    • The yeast V159N actin mutant reveals roles for actin dynamics in vivo
    • Belmont, L., and D. Drubin. 1998. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 142:1289-1299.
    • (1998) J. Cell Biol. , vol.142 , pp. 1289-1299
    • Belmont, L.1    Drubin, D.2
  • 10
    • 0024829578 scopus 로고
    • Multi-copy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the rasrelated gene RSR1
    • Bender, A., and J. Pringle. 1989. Multi-copy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the rasrelated gene RSR1. Proc. Natl. Acad. Sci. USA. 86:9976-9980.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9976-9980
    • Bender, A.1    Pringle, J.2
  • 11
    • 0027470208 scopus 로고
    • Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4
    • Brennwald, P., and P. Novick. 1993. Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature. 360:560-563.
    • (1993) Nature , vol.360 , pp. 560-563
    • Brennwald, P.1    Novick, P.2
  • 12
    • 0028107971 scopus 로고
    • What are the basic functions of microfilaments? Insights from studies in budding yeast
    • Bretscher, A., B. Drees, E. Harsay, D. Schott, and T. Wang. 1994. What are the basic functions of microfilaments? Insights from studies in budding yeast. J. Cell Biol. 126:821-825.
    • (1994) J. Cell Biol. , vol.126 , pp. 821-825
    • Bretscher, A.1    Drees, B.2    Harsay, E.3    Schott, D.4    Wang, T.5
  • 14
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R., and G. Joyce. 1992. Randomization of genes by PCR mutagenesis. PCR Methods and Applications. 2:28-33.
    • (1992) PCR Methods and Applications , vol.2 , pp. 28-33
    • Cadwell, R.1    Joyce, G.2
  • 15
    • 0028931727 scopus 로고
    • Patterns of bud-site selection in the yeast Saccharomyces cerevisiae
    • Chant, J., and J. Pringle. 1995. Patterns of bud-site selection in the yeast Saccharomyces cerevisiae. J. Cell Biol. 129:751-765.
    • (1995) J. Cell Biol. , vol.129 , pp. 751-765
    • Chant, J.1    Pringle, J.2
  • 16
    • 0028954614 scopus 로고
    • Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions
    • Drees, B., C. Brown, B. Barrell, and A. Bretscher. 1995. Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions. J. Cell Biol. 28:383-392.
    • (1995) J. Cell Biol. , vol.28 , pp. 383-392
    • Drees, B.1    Brown, C.2    Barrell, B.3    Bretscher, A.4
  • 17
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D., and WJ. Nelson. 1996. Origins of cell polarity. Cell. 84:335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.1    Nelson, W.J.2
  • 19
    • 0031444358 scopus 로고    scopus 로고
    • An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast
    • Epp, J., and J. Chant. 1997. An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast. Curr. Biol. 7:921-929.
    • (1997) Curr. Biol. , vol.7 , pp. 921-929
    • Epp, J.1    Chant, J.2
  • 20
    • 0018925667 scopus 로고
    • Localized secretion of acid-phosphatase reflects the pattern of cell growth in Saccharomyces cerevisiae
    • Field, C., and R. Schekman. 1980. Localized secretion of acid-phosphatase reflects the pattern of cell growth in Saccharomyces cerevisiae. J. Cell Biol. 86: 123-128.
    • (1980) J. Cell Biol. , vol.86 , pp. 123-128
    • Field, C.1    Schekman, R.2
  • 21
    • 0031852067 scopus 로고    scopus 로고
    • Spatial regulation of exocytosis: Lessons from yeast
    • Finger, F., and P. Novick. 1998. Spatial regulation of exocytosis: lessons from yeast. J. Cell Biol. 142:609-612.
    • (1998) J. Cell Biol. , vol.142 , pp. 609-612
    • Finger, F.1    Novick, P.2
  • 22
    • 0032548828 scopus 로고    scopus 로고
    • Sec3p is a spatial landmark for polarized secretion in budding yeast
    • Finger, F., T. Hughes, and P. Novick. 1998. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell. 92:559-571.
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.1    Hughes, T.2    Novick, P.3
  • 23
    • 0025279437 scopus 로고
    • Efficient production of chicken egg yolk antibodies against a conserved mammalian protein
    • Gassmann, M., P. Thömmes, T. Weiser, and U. Hübscher. 1990. Efficient production of chicken egg yolk antibodies against a conserved mammalian protein. FASEB (Fed. Am. Soc. Exp. Biol.) J. 4:2528-2532.
    • (1990) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.4 , pp. 2528-2532
    • Gassmann, M.1    Thömmes, P.2    Weiser, T.3    Hübscher, U.4
  • 24
    • 0031980575 scopus 로고    scopus 로고
    • Endocytic internalization in yeast and animal cells: Similar and different
    • Geli, M.I., and H. Riezman. 1998. Endocytic internalization in yeast and animal cells: similar and different. J. Cell Sci. 111:1031-1037.
    • (1998) J. Cell Sci. , vol.111 , pp. 1031-1037
    • Geli, M.I.1    Riezman, H.2
  • 25
    • 0029984773 scopus 로고    scopus 로고
    • Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
    • Goodson, H., B. Anderson, H. Warrick, L. Pon, and J. Spudich. 1996. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J. Cell Biol. 133:1277-1291.
    • (1996) J. Cell Biol. , vol.133 , pp. 1277-1291
    • Goodson, H.1    Anderson, B.2    Warrick, H.3    Pon, L.4    Spudich, J.5
  • 26
    • 0024276923 scopus 로고
    • A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast
    • Goud, B., A. Salimen, N. Walworth, and P. Novick. 1988. A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast. Cell. 53:753-768.
    • (1988) Cell , vol.53 , pp. 753-768
    • Goud, B.1    Salimen, A.2    Walworth, N.3    Novick, P.4
  • 27
    • 0028902506 scopus 로고
    • The role of Myo2p, a yeast class V myosin, in vesicular transport
    • Govindan, B., R. Bowser, and P. Novick. 1995. The role of Myo2p, 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
  • 28
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E., and A. Bretscher. 1995. Parallel secretory pathways to the cell surface in yeast. J. Cell Biol. 131:297-310.
    • (1995) J. Cell Biol. , vol.131 , pp. 297-310
    • Harsay, E.1    Bretscher, A.2
  • 29
    • 0028019430 scopus 로고
    • Rapid protein extraction from Saccharomyces cerevisiae
    • Horvath, A., and H. Riezman. 1994. Rapid protein extraction from Saccharomyces cerevisiae. Yeast. 10:1305-1310.
    • (1994) Yeast , vol.10 , pp. 1305-1310
    • Horvath, A.1    Riezman, H.2
  • 30
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacterial. 153:163-168.
    • (1983) J. Bacterial. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Kimura, A.3
  • 31
    • 0025363198 scopus 로고
    • Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity
    • Johnson, D., and J. Pringle. 1990. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111:143-152.
    • (1990) J. Cell Biol. , vol.111 , pp. 143-152
    • Johnson, D.1    Pringle, J.2
  • 32
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston, G., J. Prendergast, and R. 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.1    Prendergast, J.2    Singer, R.3
  • 33
    • 0030609126 scopus 로고    scopus 로고
    • SRO9, a multisopy suppressor of the bud growth defect in the Saccharomyces cerevisiae rho3-deficient cells, shows strong genetic interactions with tropomyosin genes, suggesting its role in organization of the actin cytoskeleton
    • Kagami, M., A. Toh-e, and Y. Matsui. 1997. SRO9, a multisopy suppressor of the bud growth defect in the Saccharomyces cerevisiae rho3-deficient cells, shows strong genetic interactions with tropomyosin genes, suggesting its role in organization of the actin cytoskeleton. Genetics. 147:1003-1016.
    • (1997) Genetics , vol.147 , pp. 1003-1016
    • Kagami, M.1    Toh-e, A.2    Matsui, Y.3
  • 34
    • 0025277750 scopus 로고
    • Distinct sets of SEC genes govern vesicle formation and fusion early in the secretory pathway
    • Kaiser, C., and R. Schekman. 1990. Distinct sets of SEC genes govern vesicle formation and fusion early in the secretory pathway. Cell. 61:723-733.
    • (1990) Cell , vol.61 , pp. 723-733
    • Kaiser, C.1    Schekman, R.2
  • 35
    • 0032555918 scopus 로고    scopus 로고
    • Assembly and function of the actin cytoskeleton of yeast: Relationships between cables and patches
    • Karpova, T., J. McNally, S. Moltz, and J. Cooper. 1998. Assembly and function of the actin cytoskeleton of yeast: relationships between cables and patches. J. Cell Biol. 142:1501-1517.
    • (1998) J. Cell Biol. , vol.142 , pp. 1501-1517
    • Karpova, T.1    McNally, J.2    Moltz, S.3    Cooper, J.4
  • 36
    • 0031457805 scopus 로고    scopus 로고
    • Post-Golgi biosynthetic trafficking
    • Keller, P., and K. Simons. 1997. Post-Golgi biosynthetic trafficking. J. Cell Set. 110:3001-3009.
    • (1997) J. Cell Set. , vol.110 , pp. 3001-3009
    • Keller, P.1    Simons, K.2
  • 38
    • 0028915943 scopus 로고
    • A cell cycle checkpoint monitors cell morphogenesis in budding yeast
    • Lew, D., and S. Reed. 1995. A cell cycle checkpoint monitors cell morphogenesis in budding yeast. J. Cell Biol. 129:739-749.
    • (1995) J. Cell Biol. , vol.129 , pp. 739-749
    • Lew, D.1    Reed, S.2
  • 39
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smylp, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie, S., and S. Brown. 1994. Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smylp, 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.1    Brown, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.