메뉴 건너뛰기




Volumn 11, Issue 4, 2000, Pages 1345-1356

A screen for dominant negative mutants of SEC18 reveals a role for the AAA protein consensus sequence in ATP hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; FUNGAL PROTEIN; HYBRID PROTEIN;

EID: 0034081183     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.4.1345     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 0030807931 scopus 로고    scopus 로고
    • Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
    • Barlowe, C. (1997). Coupled ER to Golgi transport reconstituted with purified cytosolic proteins. J. Cell Biol. 139, 1097-1108.
    • (1997) J. Cell Biol. , vol.139 , pp. 1097-1108
    • Barlowe, C.1
  • 2
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by a-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard, R.J.O., Morgan, A., and Burgoyne, R.D. (1997). Stimulation of NSF ATPase activity by a-SNAP is required for SNARE complex disassembly and exocytosis. J. Cell Biol. 139, 875-883.
    • (1997) J. Cell Biol. , vol.139 , pp. 875-883
    • Barnard, R.J.O.1    Morgan, A.2    Burgoyne, R.D.3
  • 4
    • 0032054866 scopus 로고    scopus 로고
    • Analysis of regulated exocytosis in adrenal chromaffin cells: Insights into NSF/SNAP/SNARE function
    • Burgoyne, R.D., and Morgan, A. (1998). Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE function. BioEssays 20, 328-335.
    • (1998) BioEssays , vol.20 , pp. 328-335
    • Burgoyne, R.D.1    Morgan, A.2
  • 5
    • 0029767928 scopus 로고    scopus 로고
    • A possible predocking attachment site for N-ethylmaleimide-sensitive fusion protein
    • Colombo, M.I., Taddese, M., Whiteheart, S.W., and Stahl, P.D. (1996). A possible predocking attachment site for N-ethylmaleimide-sensitive fusion protein. J. Biol. Chem. 271, 18810-18816.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18810-18816
    • Colombo, M.I.1    Taddese, M.2    Whiteheart, S.W.3    Stahl, P.D.4
  • 6
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F., and Duguet, M. (1995). A 200-amino acid ATPase module in search of a basic function. BioEssays 17, 639-650.
    • (1995) BioEssays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 7
    • 0024094923 scopus 로고
    • Characterization of a component of the yeast secretory machinery: Identification of the SEC18 gene product
    • Eakle, K.A., Bernstein, M., and Emr, S.D. (1988). Characterization of a component of the yeast secretory machinery: identification of the SEC18 gene product. Mol. Cell. Biol. 8, 4098-4109.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4098-4109
    • Eakle, K.A.1    Bernstein, M.2    Emr, S.D.3
  • 8
    • 0242556207 scopus 로고
    • Mutator strains of Escherichia coli, mutD and dnaQ, with defective exonucleolytic editing by DNA polymerase III holoenzyme
    • Echols, H., Lu, C., and Burgers, P.M.J. (1983). Mutator strains of Escherichia coli, mutD and dnaQ, with defective exonucleolytic editing by DNA polymerase III holoenzyme. Proc. Natl. Acad. Sci. USA 80, 2189-2192.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2189-2192
    • Echols, H.1    Lu, C.2    Burgers, P.M.J.3
  • 9
    • 0003000807 scopus 로고    scopus 로고
    • Tools of the trade: Use of dominant-inhibitory mutants of Ras-family GTPases
    • Feig, L.A. (1999). Tools of the trade: use of dominant-inhibitory mutants of Ras-family GTPases. Nat. Cell Biol. 1, E25-E27.
    • (1999) Nat. Cell Biol. , vol.1
    • Feig, L.A.1
  • 10
    • 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
  • 12
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R.D., and Sugino, A. (1988). New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 13
    • 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
  • 14
    • 0026692898 scopus 로고
    • The yeast SEC17 gene product is functionally equivalent to mammalian alpha-snap protein
    • Griff, I.C., Schekman, R.W., Rothman, J.E., and Kaiser, C.A. (1992). The yeast SEC17 gene product is functionally equivalent to mammalian alpha-snap protein. J. Biol. Chem. 267, 12106-12115.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12106-12115
    • Griff, I.C.1    Schekman, R.W.2    Rothman, J.E.3    Kaiser, C.A.4
  • 15
    • 0030015868 scopus 로고    scopus 로고
    • Homotypic vacuole fusion requires Sec17p (yeast a-SNAP) and Sec18p (yeast NSF)
    • Haas, A., and Wickner, W. (1996). Homotypic vacuole fusion requires Sec17p (yeast a-SNAP) and Sec18p (yeast NSF). EMBO J. 15, 3296-3305.
    • (1996) EMBO J. , vol.15 , pp. 3296-3305
    • Haas, A.1    Wickner, W.2
  • 16
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexed 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 complexed 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
  • 17
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz, I. (1987). Functional inactivation of genes by dominant negative mutations. Nature 329, 219-222.
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 18
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerisation domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C.V., Steinmann, D., Whiteheart, S.W., and Weis, W.I. (1998). Crystal structure of the hexamerisation domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-563.
    • (1998) Cell , vol.94 , pp. 525-563
    • Lenzen, C.V.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 19
    • 0032142949 scopus 로고    scopus 로고
    • Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly
    • Littleton, J.T., Chapman, E.R., Kreber, R., Garment, M.B., Carlson, S.D., and Ganetzky, B. (1998). Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly. Neuron 21, 401-413.
    • (1998) Neuron , vol.21 , pp. 401-413
    • Littleton, J.T.1    Chapman, E.R.2    Kreber, R.3    Garment, M.B.4    Carlson, S.D.5    Ganetzky, B.6
  • 20
    • 0031576237 scopus 로고    scopus 로고
    • N-Ethylmaleimide-sensitive fusion protein contains high and low affinity ATP-binding sites that are functionally distinct
    • Matveeva, E.A., He, P., and Whiteheart, S.W. (1997). N-Ethylmaleimide-sensitive fusion protein contains high and low affinity ATP-binding sites that are functionally distinct. J. Biol. Chem. 272, 26413-26418.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26413-26418
    • Matveeva, E.A.1    He, P.2    Whiteheart, S.W.3
  • 21
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (a-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W., and Haas, A. (1996). Sec18p (NSF)-driven release of Sec17p (a-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 22
    • 0031774206 scopus 로고    scopus 로고
    • Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER
    • McClellan, A.J., Endres, J.B., Vogel, J.P., Palazzi, D., Rose, M.D., and Brodsky, J.L. (1998). Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER. Mol. Biol. Cell 9, 3533-3545.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3533-3545
    • McClellan, A.J.1    Endres, J.B.2    Vogel, J.P.3    Palazzi, D.4    Rose, M.D.5    Brodsky, J.L.6
  • 24
    • 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
  • 25
    • 0028802295 scopus 로고
    • Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity
    • Nagiec, E.E., Bernstein, A., and Whiteheart, S.W. (1995). Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem. 270, 29182-29188.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29182-29188
    • Nagiec, E.E.1    Bernstein, A.2    Whiteheart, S.W.3
  • 26
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 27
    • 0019424489 scopus 로고
    • Order of events in the yeast secretory pathway
    • Novick, P., Ferro, S., and Schekman, R.W. (1981). Order of events in the yeast secretory pathway. Cell 25, 461-469.
    • (1981) Cell , vol.25 , pp. 461-469
    • Novick, P.1    Ferro, S.2    Schekman, R.W.3
  • 28
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., Field, C., and Schekman, R.W. (1980). Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21, 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.W.3
  • 29
    • 0033560750 scopus 로고    scopus 로고
    • Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion
    • Otter-Nilsson, M., Hendriks, R., Pecheur-Huet, E.-I., Hoekstra, D., and Nilsson, T. (1999). Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion. EMBO J. 18, 2074-2083.
    • (1999) EMBO J. , vol.18 , pp. 2074-2083
    • Otter-Nilsson, M.1    Hendriks, R.2    Pecheur-Huet, E.-I.3    Hoekstra, D.4    Nilsson, T.5
  • 30
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel, S., and Latterich, M. (1998). The AAA team: related ATPases with diverse functions. Trends Cell Biol. 8, 65-71.
    • (1998) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 32
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-62.
    • (1994) Nature , vol.372 , pp. 55-62
    • Rothman, J.E.1
  • 34
    • 0033564941 scopus 로고    scopus 로고
    • Biochemical analysis of the Saccharomyces cerevisiae Sec18 gene product: Implications for the molecular mechanism of membrane fusion
    • Steel, G.J., Laude, A.J., Boojawan, A., Harvey, D.J., and Morgan, A. (1999). Biochemical analysis of the Saccharomyces cerevisiae Sec18 gene product: implications for the molecular mechanism of membrane fusion. Biochemistry 38, 7764-7772.
    • (1999) Biochemistry , vol.38 , pp. 7764-7772
    • Steel, G.J.1    Laude, A.J.2    Boojawan, A.3    Harvey, D.J.4    Morgan, A.5
  • 35
    • 0032512809 scopus 로고    scopus 로고
    • Selective stimulation of the D1 ATPase domain of N-ethylmaleimide-sensitive fusion protein (NSF) by soluble NSF attachment proteins
    • Steel, G.J., and Morgan, A. (1998). Selective stimulation of the D1 ATPase domain of N-ethylmaleimide-sensitive fusion protein (NSF) by soluble NSF attachment proteins. FEBS Lett. 423, 113-116.
    • (1998) FEBS Lett. , vol.423 , pp. 113-116
    • Steel, G.J.1    Morgan, A.2
  • 36
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof, T.C. (1995). The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.C.1
  • 37
    • 0028096570 scopus 로고
    • Role of two nucleotide-binding regions in a N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport
    • Sumida, M., Hong, R.M., and Tagaya, M. (1994). Role of two nucleotide-binding regions in a N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport. J. Biol. Chem. 269, 20636-20641.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20636-20641
    • Sumida, M.1    Hong, R.M.2    Tagaya, M.3
  • 39
    • 0028132782 scopus 로고
    • N-Ethylmalemide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S.W., Rossnagel, K., Buhrow, S.A., Brunner, M., Jaenicke, R., and Rothman, J.E. (1994). N-Ethylmalemide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126, 945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 41
    • 0030992881 scopus 로고    scopus 로고
    • The roles of NSF, SNAPs and SNAREs during membrane fusion
    • Woodman, P.G. (1997). The roles of NSF, SNAPs and SNAREs during membrane fusion. Biochim. Biophys. Acta 1357, 155-172.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 155-172
    • Woodman, P.G.1
  • 42
    • 0032568798 scopus 로고    scopus 로고
    • LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion
    • Xu, Z., Sato, K., and Wickner, W. (1998). LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell 93, 1125-1134.
    • (1998) Cell , vol.93 , pp. 1125-1134
    • Xu, Z.1    Sato, K.2    Wickner, W.3
  • 43
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R.C., Hanson, P.I., Jahn, R., and Brunger, A.T. (1998). Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5, 803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.