메뉴 건너뛰기




Volumn 9, Issue 12, 2002, Pages 950-957

Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; NUCLEOTIDE; PHOSPHATIDYLINOSITOL; PROTEIN P97; UNCLASSIFIED DRUG;

EID: 18744414494     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb872     Document Type: Article
Times cited : (188)

References (48)
  • 1
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec 18p and NSF
    • Peters, J., Walsh, M.J. & Franke, W.W. An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J. 9, 1757-1767 (1990).
    • (1990) EMBO J. , vol.9 , pp. 1757-1767
    • Peters, J.1    Walsh, M.J.2    Franke, W.W.3
  • 2
    • 0032489499 scopus 로고    scopus 로고
    • Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • Rabouille, C. et al. Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 92, 603-610 (1998).
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1
  • 3
    • 0033836581 scopus 로고    scopus 로고
    • Role of p97 and syntaxin-5 in the assembly of transitional endoplasmic reticulum
    • Roy, L. et al. Role of p97 and syntaxin-5 in the assembly of transitional endoplasmic reticulum. Mol. Biol. Cell 11, 2529-2542 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2529-2542
    • Roy, L.1
  • 4
    • 0035195012 scopus 로고    scopus 로고
    • Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly
    • Hetzer, M. et al. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nature Cell Biol. 3, 1086-1091 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 1086-1091
    • Hetzer, M.1
  • 5
    • 0033451992 scopus 로고    scopus 로고
    • Synergistic roles for Pim-1 and c-Myc in STAT3-mediated cell cycle progression and antiapoptosis
    • Shirogane, T. et al. Synergistic roles for Pim-1 and c-Myc in STAT3-mediated cell cycle progression and antiapoptosis. Immunity 11, 709-719 (1999).
    • (1999) Immunity , vol.11 , pp. 709-719
    • Shirogane, T.1
  • 6
    • 0030667206 scopus 로고    scopus 로고
    • A yeast mutant showing diagnostic markers of early and late apoptosis
    • Madeo, F., Fröhlich, E. & Fröhlich, K. A yeast mutant showing diagnostic markers of early and late apoptosis. J. Cell Biol. 139, 729-734 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 729-734
    • Madeo, F.1    Fröhlich, E.2    Fröhlich, K.3
  • 7
    • 0031932987 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of cdc 48p
    • Madeo, F., Schlauer, J., Zischka, H., Mecke, D. & Fröhlich, K. Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of cdc48p. Mol. Biol. Cell 9, 131-141 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 131-141
    • Madeo, F.1    Schlauer, J.2    Zischka, H.3    Mecke, D.4    Fröhlich, K.5
  • 8
    • 0033959478 scopus 로고    scopus 로고
    • p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication
    • Yamada, T. et al. p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication. FEBS Lett. 466, 287-291 (2000).
    • (2000) FEBS Lett. , vol.466 , pp. 287-291
    • Yamada, T.1
  • 9
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα
    • Dai, R.M., Chen, E., Longo, D.L., Gorbea, C.M. & Li, C.H. Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα. J. Biol. Chem. 273, 3562-3573 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.H.5
  • 10
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer, H.H., Shorter, J.G., Seemann, J., Pappin, D. & Warren, G. A complex of mammalian ufd1 and np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19, 2181-2192 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 11
    • 0034548716 scopus 로고    scopus 로고
    • Involvement of the ubiquitin-proteasome pathway in the degradation of nontyrosine kinase-type cytokine receptors of IL-9, IL-2, and erythropoietin
    • Yen, C. et al. Involvement of the ubiquitin-proteasome pathway in the degradation of nontyrosine kinase-type cytokine receptors of IL-9, IL-2, and erythropoietin. J. Immunol. 165, 6372-6380 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 6372-6380
    • Yen, C.1
  • 12
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai, R.M. & Li, C.H. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nature Cell Biol. 3, 740-744 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.H.2
  • 13
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase cdc4B/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H.H. & Rapoport, T.A. The AAA ATPase cdc4B/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656 (2001).
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 15
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch, E. et al. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nature Cell Biol. 4, 134-139 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 134-139
    • Jarosch, E.1
  • 16
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Fröhlich, K.U., Diamant, N. & Bar-Nun, S. AAA-ATPase p97/cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22, 626-634 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Fröhlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 17
    • 0030790695 scopus 로고    scopus 로고
    • p47 is a cofactor for p97-mediated membrane fusion
    • Kondo, H. et al. p47 is a cofactor for p97-mediated membrane fusion. Nature 388, 75-78 (1997).
    • (1997) Nature , vol.388 , pp. 75-78
    • Kondo, H.1
  • 18
    • 0032561398 scopus 로고    scopus 로고
    • The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97
    • Meyer, H.H., Kondo, H. & Warren, G. The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. FEBS Lett. 437, 255-257 (1998).
    • (1998) FEBS Lett. , vol.437 , pp. 255-257
    • Meyer, H.H.1    Kondo, H.2    Warren, G.3
  • 19
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E 4, is involved in multiubiquitin chain assembly
    • Koegl, M.T. et al. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644 (1999).
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.T.1
  • 20
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • Ghislain, M., Dohmen, R.J., Lévy, F. & Varshavsky, A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 15, 4884-4899 (1996).
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Lévy, F.3    Varshavsky, A.4
  • 21
    • 0035199034 scopus 로고    scopus 로고
    • AAA proteins: In search of a common molecular basis. International Meeting on Cellular Functions of AAA Proteins
    • Maurizi, M.R. & Li, C.H. AAA proteins: In search of a common molecular basis. International Meeting on Cellular Functions of AAA Proteins. EMBO Rep. 2, 980-985 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 980-985
    • Maurizi, M.R.1    Li, C.H.2
  • 22
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel, S. & Latterich, M. The AAA team: Related ATPases with diverse functions. Trends Cell. Biol. 8, 65-71 (1998).
    • (1998) Trends Cell. Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 23
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A.F., Aravind, L., Spouge, J.L. & Koonin, E.V. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (1999).
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 24
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure - Diverse function
    • Ogura, T. & Wilkinson, A.J. AAA+ superfamily ATPases: Common structure - Diverse function. Genes Cells 6, 575-597 (2001).
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 25
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • Vale, R.D. AAA proteins. Lords of the ring. J. Cell Biol. 10, F13-19 (2000).
    • (2000) J. Cell Biol. , vol.10
    • Vale, R.D.1
  • 26
    • 0033592895 scopus 로고    scopus 로고
    • Crystal structure of the Sec18p N-terminal domain
    • Babor, S.M. & Fass, D. Crystal structure of the Sec18p N-terminal domain. Proc. Natl. Acad. Sci. USA 96, 14759-14764 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14759-14764
    • Babor, S.M.1    Fass, D.2
  • 27
    • 0033592545 scopus 로고    scopus 로고
    • The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple βαββ element
    • Coles, M. et al. The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple βαββ element. Curr. Biol. 9, 1158-1168 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1158-1168
    • Coles, M.1
  • 28
    • 0033163807 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of N-ethylmaleimide-sensitive fusion protein
    • May, A.P., Misura, K.M.S., Whiteheart, S.W. & Weis, W.I. Crystal structure of the N-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nature Cell Biol. 1, 175-182 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 175-182
    • May, A.P.1    Misura, K.M.S.2    Whiteheart, S.W.3    Weis, W.I.4
  • 29
    • 0033165864 scopus 로고    scopus 로고
    • NSF N-terminal domain crystal structure: Models of NSF function
    • Yu, R.C., Jahn, R., & Brunger, A.T. NSF N-terminal domain crystal structure: Models of NSF function. Mol. Cell 4, 97-107 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 97-107
    • Yu, R.C.1    Jahn, R.2    Brunger, A.T.3
  • 30
    • 0034502514 scopus 로고    scopus 로고
    • Structure of the AAA ATPase p97
    • Zhang X., et al. Structure of the AAA ATPase p97. Mol. Cell 6, 1473-1484 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1473-1484
    • Zhang, X.1
  • 31
    • 0026500709 scopus 로고
    • 2+-ATPase complex. A structural study
    • 2+-ATPase complex. A structural study. J. Mol. Biol. 223, 557-571 (1992).
    • (1992) J. Mol. Biol. , vol.223 , pp. 557-571
    • Peters, J.1
  • 32
    • 0032909548 scopus 로고    scopus 로고
    • Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography
    • Rockel, B. et al. Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography. FEBS Lett. 451, 27-32 (1999).
    • (1999) FEBS Lett. , vol.451 , pp. 27-32
    • Rockel, B.1
  • 34
    • 0036295232 scopus 로고    scopus 로고
    • Electron cryo-microscopy of VAT, the archaeal p97/CDC 48 homologue from Thermoplasma acidophilum
    • Rockel, B., Jakana, J., Chiu, W. & Baumeister, W. Electron cryo-microscopy of VAT, the archaeal p97/CDC48 homologue from Thermoplasma acidophilum. J. Mol. Biol. 317, 673-681 (2002).
    • (2002) J. Mol. Biol. , vol.317 , pp. 673-681
    • Rockel, B.1    Jakana, J.2    Chiu, W.3    Baumeister, W.4
  • 35
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerizatioN-domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C.U., Steinmann, D., Whiteheart, S.W. & Weis, W.I. Crystal structure of the hexamerizatioN-domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536 (1998).
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 36
    • 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. & Brunger, A.T. Structure of the ATP-dependent oligomerizatioN-domain of N-ethylmaleimide sensitive factor complexed with ATP. Nature Struct. Biol. 5, 803-811 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 37
    • 0031282504 scopus 로고    scopus 로고
    • Signaling mechanistics: Aluminum fluoride for molecule of the year
    • Wittinghofer, A. Signaling mechanistics: Aluminum fluoride for molecule of the year. Curr. Biol. 7, R682-685 (1997).
    • (1997) Curr. Biol. , vol.7
    • Wittinghofer, A.1
  • 38
    • 0035839032 scopus 로고    scopus 로고
    • Structure and mechanism of the RuvB Holliday junction branch migration motor
    • Putnam, C.D. et al. Structure and mechanism of the RuvB Holliday junction branch migration motor. J. Mol. Biol. 311, 297-310 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 297-310
    • Putnam, C.D.1
  • 39
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HsIUV protease-chaperone complex
    • Sousa, M.C. et al. Crystal and solution structures of an HsIUV protease-chaperone complex. Cell 103, 633-643 (2000).
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1
  • 40
  • 41
    • 0035783135 scopus 로고    scopus 로고
    • A corrected quaternary arrangement of the peptidase HsIV and ATPase HsIU in a cocrystal structure
    • Wang, J. A corrected quaternary arrangement of the peptidase HsIV and ATPase HsIU in a cocrystal structure. J. Struct. Biol. 134, 15-24 (2001).
    • (2001) J. Struct. Biol. , vol.134 , pp. 15-24
    • Wang, J.1
  • 42
    • 0035184442 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in a protease-associated ATPase HslU
    • Wang, J. et al. Nucleotide-dependent conformational changes in a protease-associated ATPase HslU. Structure 9, 1107-1116 (2001).
    • (2001) Structure , vol.9 , pp. 1107-1116
    • Wang, J.1
  • 43
    • 0035877720 scopus 로고    scopus 로고
    • Functional analysis of the trypanosomal AAA protein TbVCP with trans-dominant ATP hydrolysis mutants
    • Lamb, J.R., Fu, V., Wirtz, E. & Bangs, J.D. Functional analysis of the trypanosomal AAA protein TbVCP with trans-dominant ATP hydrolysis mutants. J. Biol. Chem. 276, 21512-21520 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21512-21520
    • Lamb, J.R.1    Fu, V.2    Wirtz, E.3    Bangs, J.D.4
  • 44
    • 0031042544 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of VAT, a CDC48/p 97 ATPase homologue from the archaeon Thermoplasma acidophilum
    • Pamnani, V. et al. Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum. FEBS Lett. 404, 263-268 (1997).
    • (1997) FEBS Lett. , vol.404 , pp. 263-268
    • Pamnani, V.1
  • 45
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER WEB: Processing and visualization of images in 3D EM and related fields
    • Frank, J. & Radermacher, M. SPIDER and WEB: Processing and visualization of images in 3D EM and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2
  • 46
    • 0039149525 scopus 로고    scopus 로고
    • The effect of overabundant projection directions on 3D reconstruction algorithms
    • Sorzano, C.O.S. et al. The effect of overabundant projection directions on 3D reconstruction algorithms. J. Struct. Biol. 133, 108-118 (2001).
    • (2001) J. Struct. Biol. , vol.133 , pp. 108-118
    • Sorzano, C.O.S.1
  • 47
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers, W., Milligan, R.A. & McCammon, J.A. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125, 185-195 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 48
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.