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Volumn 16, Issue 9, 2005, Pages 3963-3977

Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEIN; PROTEIN DSL1P; PROTEIN DSL3; PROTEIN TIP20P; PROTEIN UFE1P; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 24344480456     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-01-0056     Document Type: Article
Times cited : (93)

References (82)
  • 1
    • 8344255773 scopus 로고    scopus 로고
    • Tracking SNARE complex formation in live endocrine cells
    • An, S. J., and Almers, W. (2004). Tracking SNARE complex formation in live endocrine cells. Science 306, 1042-1046.
    • (2004) Science , vol.306 , pp. 1042-1046
    • An, S.J.1    Almers, W.2
  • 2
    • 0035914416 scopus 로고    scopus 로고
    • The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast
    • Andag, U., Neumann, T., and Schmitt, H. D. (2001). The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J. Biol. Chem. 276, 39150-39160.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39150-39160
    • Andag, U.1    Neumann, T.2    Schmitt, H.D.3
  • 3
    • 0347695021 scopus 로고    scopus 로고
    • Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat
    • Andag, U., and Schmitt, H. D. (2003). Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat. J. Biol. Chem. 278, 51722-51734.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51722-51734
    • Andag, U.1    Schmitt, H.D.2
  • 4
    • 0027097849 scopus 로고
    • The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • Antebi, A., and Fink, G. R. (1992). The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 3, 633-654.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 5
    • 0036166318 scopus 로고    scopus 로고
    • Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
    • Antonin, W., Fasshauer, D., Becker, S., Jahn, R., and Schneider, T. R. (2002). Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs. Nat. Struct. Biol. 9, 107-111.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 107-111
    • Antonin, W.1    Fasshauer, D.2    Becker, S.3    Jahn, R.4    Schneider, T.R.5
  • 6
    • 0031808667 scopus 로고    scopus 로고
    • Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p
    • Ballensiefen, W., Ossipov, D., and Schmitt, H. D. (1998). Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p. J. Cell Sci. 111, 1507-1520.
    • (1998) J. Cell Sci. , vol.111 , pp. 1507-1520
    • Ballensiefen, W.1    Ossipov, D.2    Schmitt, H.D.3
  • 7
    • 0030807931 scopus 로고    scopus 로고
    • Coupled ER to Golgi transport reconstituted with purified cytosolic components
    • Barlowe, C. (1997). Coupled ER to Golgi transport reconstituted with purified cytosolic components. J. Cell Biol. 139, 1097-1108.
    • (1997) J. Cell Biol. , vol.139 , pp. 1097-1108
    • Barlowe, C.1
  • 8
    • 0034189373 scopus 로고    scopus 로고
    • Traffic COPs of the early secretory pathway
    • Barlowe, C. (2000). Traffic COPs of the early secretory pathway. Traffic 1, 371-377.
    • (2000) Traffic , vol.1 , pp. 371-377
    • Barlowe, C.1
  • 10
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock, J. B., Matern, H. T., Peden, A. A., and Scheller, R. H. (2001). A genomic perspective on membrane compartment organization. Nature 409, 839-841.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 11
    • 0036544561 scopus 로고    scopus 로고
    • A cycle of Vam7p release from and Ptdlns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion
    • Boeddinghaus, C., Merz, A. J., Laage, R., and Ungermann, C. (2002). A cycle of Vam7p release from and Ptdlns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion. J. Cell Biol. 357, 79-89.
    • (2002) J. Cell Biol. , vol.357 , pp. 79-89
    • Boeddinghaus, C.1    Merz, A.J.2    Laage, R.3    Ungermann, C.4
  • 13
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., Ballew, N., and Barlowe, C. (1998). Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 17, 2156-2165.
    • (1998) EMBO J. , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 14
    • 0033672239 scopus 로고    scopus 로고
    • Human Zw10 and ROD are mitotic checkpoint proteins that bind to kinetochores
    • Chan, G. K., Jablonski, S. A., Starr, D. A., Goldberg, M. L., and Yen, T. J. (2000). Human Zw10 and ROD are mitotic checkpoint proteins that bind to kinetochores. Nat. Cell Biol. 2, 944-947.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 944-947
    • Chan, G.K.1    Jablonski, S.A.2    Starr, D.A.3    Goldberg, M.L.4    Yen, T.J.5
  • 17
    • 1542320073 scopus 로고    scopus 로고
    • A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly
    • Fasshauer, D., and Margittai, M. (2004). A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly. J. Biol. Chem. 279, 7613-7621.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7613-7621
    • Fasshauer, D.1    Margittai, M.2
  • 18
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T., and Jahn, R. (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA 95, 15781-15786.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 19
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick, S., and Jahn, R. (1994). Vesicle fusion from yeast to man. Nature 370, 191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 20
    • 0031779253 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae early secretion mutant tip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufe1p
    • Frigerio, G. (1998). The Saccharomyces cerevisiae early secretion mutant tip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufe1p. Yeast 14, 633-646.
    • (1998) Yeast , vol.14 , pp. 633-646
    • Frigerio, G.1
  • 21
    • 0021015541 scopus 로고
    • A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product
    • Gallwitz, D., Donath, C., and Sander, C. (1983). A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product. Nature 306, 704-707.
    • (1983) Nature , vol.306 , pp. 704-707
    • Gallwitz, D.1    Donath, C.2    Sander, C.3
  • 23
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham, T. R., and Emr, S. D. (1991). Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol. 114, 207-218.
    • (1991) J. Cell Biol. , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 24
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P. I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J. E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 25
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Antibodies. A Laboratory Manual, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1988) Antibodies. A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 26
    • 0029864907 scopus 로고    scopus 로고
    • Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport
    • Harris, S. L., and Waters, M. G. (1996). Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport. J. Cell Biol 132, 985-998.
    • (1996) J. Cell Biol , vol.132 , pp. 985-998
    • Harris, S.L.1    Waters, M.G.2
  • 27
    • 0034607967 scopus 로고    scopus 로고
    • Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking
    • Hatsuzawa, K., Hirose, H., Tani, K., Yamamoto, A., Scheller, R. H., and Tagaya, M. (2000). Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking. J. Biol. Chem. 275, 13713-13720.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13713-13720
    • Hatsuzawa, K.1    Hirose, H.2    Tani, K.3    Yamamoto, A.4    Scheller, R.H.5    Tagaya, M.6
  • 31
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., Halladay, J., and Craig, E. A. (1996). Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144, 1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 32
    • 0025277750 scopus 로고
    • Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway
    • Kaiser, C. A., and Schekman, R. (1990). Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell 61, 723-733.
    • (1990) Cell , vol.61 , pp. 723-733
    • Kaiser, C.A.1    Schekman, R.2
  • 33
    • 1842482412 scopus 로고    scopus 로고
    • Tip20p prohibits back-fusion of COPlI vesicles with the endoplasmic reticulum
    • Kamena, F., and Spang, A. (2004). Tip20p prohibits back-fusion of COPlI vesicles with the endoplasmic reticulum. Science 304, 286-289.
    • (2004) Science , vol.304 , pp. 286-289
    • Kamena, F.1    Spang, A.2
  • 34
  • 35
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung, D. W., Chen, E., and Goeddel, D. V. (1989). A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique 1, 11-15.
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 36
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis, M. J., and Pelham, H.R.B. (1996). SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 85, 205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 37
    • 0030911653 scopus 로고    scopus 로고
    • A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum
    • Lewis, M. J., Rayner, J. C., and Pelham, H.R.B. (1997). A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. EMBO J. 16, 3017-3024.
    • (1997) EMBO J. , vol.16 , pp. 3017-3024
    • Lewis, M.J.1    Rayner, J.C.2    Pelham, H.R.B.3
  • 38
    • 24344440195 scopus 로고    scopus 로고
    • Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum
    • Li, Y., Gallwitz, D., and Peng, R. (2005). Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum. Mol. Biol. Cell 16, 3951-3962.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3951-3962
    • Li, Y.1    Gallwitz, D.2    Peng, R.3
  • 39
    • 0036736095 scopus 로고    scopus 로고
    • Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function
    • Liu, Y., and Barlowe, C. (2002). Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function. Mol. Biol. Cell 13, 3314-3324.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3314-3324
    • Liu, Y.1    Barlowe, C.2
  • 40
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M. P., and Bukau, B. (2005). Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol. Life Sci. 62, 670-684.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 41
    • 0034631955 scopus 로고    scopus 로고
    • Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors
    • McNew, J. A., Weber, T., Parlati, F., Johnston, R. J., Melia, T. J., Sollner, T. H., and Rothman, J. E. (2000). Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors. J. Cell Biol. 150, 105-117.
    • (2000) J. Cell Biol. , vol.150 , pp. 105-117
    • McNew, J.A.1    Weber, T.2    Parlati, F.3    Johnston, R.J.4    Melia, T.J.5    Sollner, T.H.6    Rothman, J.E.7
  • 42
    • 3142536716 scopus 로고    scopus 로고
    • Exploration of essential gene functions via titratable promoter alleles
    • Mnaimneh, S. et al. (2004). Exploration of essential gene functions via titratable promoter alleles. Cell 118, 31-44.
    • (2004) Cell , vol.118 , pp. 31-44
    • Mnaimneh, S.1
  • 43
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad, D., Hunter, R., and Parker, R. (1992). A rapid method for localized mutagenesis of yeast genes. Yeast 8, 79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 45
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000). T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 46
    • 0025891541 scopus 로고
    • The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport
    • Ossig, R., Dascher, C., Trepte, H. H., Schmitt, H. D., and Gallwitz, D. (1991). The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell. Biol. 11, 2980-2993.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2980-2993
    • Ossig, R.1    Dascher, C.2    Trepte, H.H.3    Schmitt, H.D.4    Gallwitz, D.5
  • 47
    • 0342470378 scopus 로고    scopus 로고
    • Yeast ER-Golgi v-SNAREs Bos1p and Bet1p differ in steady-state localization and targeting
    • Ossipov, D., Schroder-Kohne, S., and Schmitt, H. D. (1999). Yeast ER-Golgi v-SNAREs Bos1p and Bet1p differ in steady-state localization and targeting. J. Cell Sci. 112, 4135-4142.
    • (1999) J. Cell Sci. , vol.112 , pp. 4135-4142
    • Ossipov, D.1    Schroder-Kohne, S.2    Schmitt, H.D.3
  • 48
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis (secretion)
    • Palade, G. (1975). Intracellular aspects of the process of protein synthesis (secretion). Science 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 49
    • 0032489507 scopus 로고    scopus 로고
    • Organelle membrane fusion: A novel function for the syntaxin homolog Ufe1p in ER membrane fusion
    • Patel, S. K., Indig, F. E., Olivieri, N., Levine, N. D., and Latterich, M. (1998). Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion. Cell 92, 611-620.
    • (1998) Cell , vol.92 , pp. 611-620
    • Patel, S.K.1    Indig, F.E.2    Olivieri, N.3    Levine, N.D.4    Latterich, M.5
  • 50
    • 0035661564 scopus 로고    scopus 로고
    • Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit
    • Reilly, B. A., Kraynack, B. A., VanRheenen, S. M., and Waters, M. G. (2001). Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit. Mol. Biol. Cell 12, 3783-3796.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3783-3796
    • Reilly, B.A.1    Kraynack, B.A.2    Vanrheenen, S.M.3    Waters, M.G.4
  • 51
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., and Seraphin, B. (1999). A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 52
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
    • Roberg, K. J., Rowley, N., and Kaiser, C.A. (1997). Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. J. Cell Biol. 137, 1469-1482.
    • (1997) J. Cell Biol. , vol.137 , pp. 1469-1482
    • Roberg, K.J.1    Rowley, N.2    Kaiser, C.A.3
  • 53
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 54
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J. E., and Orci, L. (1992). Molecular dissection of the secretory pathway. Nature 355, 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 57
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J. C., Hardwick, K. G., Dean, N., and Pelham, H.R.B. (1990). ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61, 1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.B.4
  • 58
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 59
    • 0021267177 scopus 로고
    • Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: Application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots
    • Smith, D. E., and Fisher, P. A. (1984). Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots. J. Cell Biol. 99, 20-28.
    • (1984) J. Cell Biol. , vol.99 , pp. 20-28
    • Smith, D.E.1    Fisher, P.A.2
  • 60
    • 0028168008 scopus 로고
    • A Rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Segaard, M., Tani, K., Ye, R. R., Geromanos, S., Tempst, P., Kirchhausen, T., Rothman, J. E., and Söllner, T. (1994). A Rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell 78, 937-948.
    • (1994) Cell , vol.78 , pp. 937-948
    • Segaard, M.1    Tani, K.2    Ye, R.R.3    Geromanos, S.4    Tempst, P.5    Kirchhausen, T.6    Rothman, J.E.7    Söllner, T.8
  • 61
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H., and Rothman, J. E. (1993a). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 63
    • 0031852650 scopus 로고    scopus 로고
    • ZW10 helps recruit dynactin and dynein to the kinetochore
    • Starr, D. A., Williams, B. C., Hays, T. S., and Goldberg, M. L. (1998). ZW10 helps recruit dynactin and dynein to the kinetochore. J. Cell Biol. 142, 763-774.
    • (1998) J. Cell Biol. , vol.142 , pp. 763-774
    • Starr, D.A.1    Williams, B.C.2    Hays, T.S.3    Goldberg, M.L.4
  • 65
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 a resolution
    • Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. (1998). Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 66
    • 4444230642 scopus 로고    scopus 로고
    • Dynactin is involved in a checkpoint to monitor cell wall synthesis in Saccharomyces cerevisiae
    • Suzuki, M., Igarashi, R., Sekiya, M., Utsugi, T., Morishita, S., Yukawa, M., and Ohya, Y. (2004). Dynactin is involved in a checkpoint to monitor cell wall synthesis in Saccharomyces cerevisiae. Nat. Cell Biol. 6, 861-871.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 861-871
    • Suzuki, M.1    Igarashi, R.2    Sekiya, M.3    Utsugi, T.4    Morishita, S.5    Yukawa, M.6    Ohya, Y.7
  • 67
    • 0026542540 scopus 로고
    • The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system
    • Sweet, D. J., and Pelham, H. R. (1992). The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system. EMBO J. 11, 423-432.
    • (1992) EMBO J. , vol.11 , pp. 423-432
    • Sweet, D.J.1    Pelham, H.R.2
  • 68
    • 0027294075 scopus 로고
    • The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p
    • Sweet, D. J., and Pelham, H. R. (1993). The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p. EMBO J. 12, 2831-2840.
    • (1993) EMBO J. , vol.12 , pp. 2831-2840
    • Sweet, D.J.1    Pelham, H.R.2
  • 69
    • 3542999933 scopus 로고    scopus 로고
    • A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion
    • Thorngren, N., Collins, K. M., Fratti, R. A., Wickner, W., and Merz, A. J. (2004). A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. EMBO J. 23, 2765-2776.
    • (2004) EMBO J. , vol.23 , pp. 2765-2776
    • Thorngren, N.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4    Merz, A.J.5
  • 70
  • 71
    • 0034255256 scopus 로고    scopus 로고
    • A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking
    • Ungermann, C., Price, A., and Wickner, W. (2000). A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking. Proc. Natl. Acad. Sci. USA 97, 8889-8891.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8889-8891
    • Ungermann, C.1    Price, A.2    Wickner, W.3
  • 72
    • 0032101225 scopus 로고    scopus 로고
    • Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking
    • VanRheenen, S. M., Cao, X., Lupashin, V. V., Barlowe, C., and Waters, M. G. (1998). Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking. J. Cell Biol. 141, 1107-1119.
    • (1998) J. Cell Biol. , vol.141 , pp. 1107-1119
    • Vanrheenen, S.M.1    Cao, X.2    Lupashin, V.V.3    Barlowe, C.4    Waters, M.G.5
  • 73
    • 0033571293 scopus 로고    scopus 로고
    • Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p
    • VanRheenen, S. M., Cao, X., Sapperstein, S. K., Chiang, E. C., Lupashin, V. V., Barlowe, C., and Waters, M. G. (1999). Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p. J. Cell Biol. 147, 729-742.
    • (1999) J. Cell Biol. , vol.147 , pp. 729-742
    • Vanrheenen, S.M.1    Cao, X.2    Sapperstein, S.K.3    Chiang, E.C.4    Lupashin, V.V.5    Barlowe, C.6    Waters, M.G.7
  • 74
    • 0035016821 scopus 로고    scopus 로고
    • Dsl1p, an essential protein required for membrane traffic at the endoplasmic reticulum/Golgi interface in yeast
    • VanRheenen, S. M., Reilly, B. A., Chamberlain, S. J., and Waters, M. G. (2001). Dsl1p, an essential protein required for membrane traffic at the endoplasmic reticulum/Golgi interface in yeast. Traffic 2, 212-231.
    • (2001) Traffic , vol.2 , pp. 212-231
    • Vanrheenen, S.M.1    Reilly, B.A.2    Chamberlain, S.J.3    Waters, M.G.4
  • 75
    • 0034252821 scopus 로고    scopus 로고
    • Membrane tethering and fusion in the secretory and endocytic pathways
    • Waters, M. G., and Hughson, F. M. (2000). Membrane tethering and fusion in the secretory and endocytic pathways. Traffic 1, 588-597.
    • (2000) Traffic , vol.1 , pp. 588-597
    • Waters, M.G.1    Hughson, F.M.2
  • 76
    • 0025957468 scopus 로고
    • 'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters, M. G., Serafini, T., and Rothman, J. E. (1991). 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349, 248-251.
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.G.1    Serafini, T.2    Rothman, J.E.3
  • 78
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • Whyte, J. R., and Munro, S. (2002). Vesicle tethering complexes in membrane traffic. J. Cell Sci. 115, 2627-2637.
    • (2002) J. Cell Sci. , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 79
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler, E. A. et al. (1999). Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285, 901-906.
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1
  • 80
    • 0035794203 scopus 로고    scopus 로고
    • RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G(2)/M checkpoint control
    • Xiao, J., Liu, C. C., Chen, P. L., and Lee, W. H. (2001). RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G(2)/M checkpoint control. J. Biol. Chem. 276, 6105-6111.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6105-6111
    • Xiao, J.1    Liu, C.C.2    Chen, P.L.3    Lee, W.H.4
  • 81
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • Yamaguchi, T., Dulubova, I., Min, S. W., Chen, X., Rizo, J., and Südhof, T. C. (2002). Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev. Cell 2, 295-305.
    • (2002) Dev. Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3    Chen, X.4    Rizo, J.5    Südhof, T.C.6
  • 82
    • 0037898897 scopus 로고    scopus 로고
    • BNips: A group of pro-apoptotic proteins in the Bcl-2 family
    • Zhang, H. M., Cheung, P., Yanagawa, B., McManus, B. M., and Yang, D. C. (2003). BNips: a group of pro-apoptotic proteins in the Bcl-2 family. Apoptosis 8, 229-236.
    • (2003) Apoptosis , vol.8 , pp. 229-236
    • Zhang, H.M.1    Cheung, P.2    Yanagawa, B.3    McManus, B.M.4    Yang, D.C.5


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