메뉴 건너뛰기




Volumn 8, Issue 1, 2005, Pages 86-92

The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; VEGETABLE PROTEIN;

EID: 11844277123     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2004.11.012     Document Type: Review
Times cited : (168)

References (50)
  • 1
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • J.C. Young, I. Moarefi, and F.U. Hartl Hsp90: a specialized but essential protein-folding tool J Cell Biol 154 2001 267 273
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 2
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • D. Picard Heat-shock protein 90, a chaperone for folding and regulation Cell Mol Life Sci 59 2002 1640 1648
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 4
    • 0033529033 scopus 로고    scopus 로고
    • Molecular chaperones: The busy life of Hsp90
    • M.P. Mayer, and B. Bukau Molecular chaperones: the busy life of Hsp90 Curr Biol 9 1999 R322 R325
    • (1999) Curr Biol , vol.9
    • Mayer, M.P.1    Bukau, B.2
  • 5
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • J. Frydman Folding of newly translated proteins in vivo: the role of molecular chaperones Annu Rev Biochem 70 2001 603 647
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 6
    • 0034817255 scopus 로고    scopus 로고
    • The Hsp90 family of proteins in Arabidopsis thaliana
    • P. Krishna, and G. Gloor The Hsp90 family of proteins in Arabidopsis thaliana Cell Stress Chaperones 6 2001 238 246
    • (2001) Cell Stress Chaperones , vol.6 , pp. 238-246
    • Krishna, P.1    Gloor, G.2
  • 7
    • 0028675649 scopus 로고
    • Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-family gene HSP81
    • N. Yabe, T. Takahashi, and Y. Komeda Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-family gene HSP81 Plant Cell Physiol 35 1994 1207 1219
    • (1994) Plant Cell Physiol , vol.35 , pp. 1207-1219
    • Yabe, N.1    Takahashi, T.2    Komeda, Y.3
  • 8
    • 0141705339 scopus 로고    scopus 로고
    • HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis
    • A. Takahashi, C. Casais, K. Ichimura, and K. Shirasu HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis Proc Natl Acad Sci USA 100 2003 11777 11782 The authors show that a T-DNA insertion in hsp90.1 compromises RPS2- but not RPM1-mediated disease resistance. Genetic and biochemical analyses identified RAR1 and SGT1 as HSP90 interactors. Domain deletion analysis determined the interacting portions of the proteins.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11777-11782
    • Takahashi, A.1    Casais, C.2    Ichimura, K.3    Shirasu, K.4
  • 9
    • 0242556837 scopus 로고    scopus 로고
    • Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
    • D.A. Hubert, P. Tornero, Y. Belkhadir, P. Krishna, A. Takahashi, K. Shirasu, and J.L. Dangl Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein EMBO J 22 2003 5679 5689 A detailed analysis and excellent discussion of HSP90's role in disease resistance. The authors characterize the hsp90.2-3 mutation and demonstrate that it compromises RPM1 but not RPS2 function. RAR1 and SGT1 are identified as potential HSP90 co-chaperones through biochemical analysis.
    • (2003) EMBO J , vol.22 , pp. 5679-5689
    • Hubert, D.A.1    Tornero, P.2    Belkhadir, Y.3    Krishna, P.4    Takahashi, A.5    Shirasu, K.6    Dangl, J.L.7
  • 10
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • C. Queitsch, T.A. Sangster, and S. Lindquist Hsp90 as a capacitor of phenotypic variation Nature 417 2002 618 624
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 11
    • 0346034697 scopus 로고    scopus 로고
    • The chlorate-resistant and photomorphogenesis-defective mutant cr88 encodes a chloroplast-targeted HSP90
    • D. Cao, J.E. Froehlich, H. Zhang, and C.L. Cheng The chlorate-resistant and photomorphogenesis-defective mutant cr88 encodes a chloroplast-targeted HSP90 Plant J 33 2003 107 118 The authors identify a mutated chloroplast hsp90.5 as causal to the cr88 phenotype. Whether HSP90.5 aids in chloroplast protein import or functions in folding within the stroma has not yet been determined.
    • (2003) Plant J , vol.33 , pp. 107-118
    • Cao, D.1    Froehlich, J.E.2    Zhang, H.3    Cheng, C.L.4
  • 12
    • 0030904362 scopus 로고    scopus 로고
    • A chlorate-resistant mutant defective in the regulation of nitrate reductase gene expression in Arabidopsis defines a new HY locus
    • Y. Lin, and C.L. Cheng A chlorate-resistant mutant defective in the regulation of nitrate reductase gene expression in Arabidopsis defines a new HY locus Plant Cell 9 1997 21 35
    • (1997) Plant Cell , vol.9 , pp. 21-35
    • Lin, Y.1    Cheng, C.L.2
  • 13
    • 0034143409 scopus 로고    scopus 로고
    • Genetic interactions between the chlorate-resistant mutant cr88 and the photomorphogenic mutants cop1 and hy5
    • D. Cao, Y. Lin, and C.L. Cheng Genetic interactions between the chlorate-resistant mutant cr88 and the photomorphogenic mutants cop1 and hy5 Plant Cell 12 2000 199 210
    • (2000) Plant Cell , vol.12 , pp. 199-210
    • Cao, D.1    Lin, Y.2    Cheng, C.L.3
  • 14
    • 0036500154 scopus 로고    scopus 로고
    • SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins
    • S. Ishiguro, Y. Watanabe, N. Ito, H. Nonaka, N. Takeda, T. Sakai, H. Kanaya, and K. Okada SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins EMBO J 21 2002 898 908
    • (2002) EMBO J , vol.21 , pp. 898-908
    • Ishiguro, S.1    Watanabe, Y.2    Ito, N.3    Nonaka, H.4    Takeda, N.5    Sakai, T.6    Kanaya, H.7    Okada, K.8
  • 15
    • 0037001929 scopus 로고    scopus 로고
    • Shoot and floral meristem maintenance in Arabidopsis
    • J.C. Fletcher Shoot and floral meristem maintenance in Arabidopsis Annu Rev Plant Biol 53 2002 45 66
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 45-66
    • Fletcher, J.C.1
  • 16
    • 0038032933 scopus 로고    scopus 로고
    • Plant meristems: A merry-go-round of signals
    • P. Doerner Plant meristems: a merry-go-round of signals Curr Biol 13 2003 R368 R374
    • (2003) Curr Biol , vol.13
    • Doerner, P.1
  • 17
    • 0030054166 scopus 로고    scopus 로고
    • Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90
    • L.F. Stancato, K.A. Hutchison, P. Krishna, and W.B. Pratt Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90 Biochemistry 35 1996 554 561
    • (1996) Biochemistry , vol.35 , pp. 554-561
    • Stancato, L.F.1    Hutchison, K.A.2    Krishna, P.3    Pratt, W.B.4
  • 18
  • 19
    • 0035205522 scopus 로고    scopus 로고
    • Hsp90-binding immunophilins in plants: The protein movers
    • W.B. Pratt, P. Krishna, and L.J. Olsen Hsp90-binding immunophilins in plants: the protein movers Trends Plant Sci 6 2001 54 58
    • (2001) Trends Plant Sci , vol.6 , pp. 54-58
    • Pratt, W.B.1    Krishna, P.2    Olsen, L.J.3
  • 20
    • 0035937462 scopus 로고    scopus 로고
    • Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40
    • T.Z. Berardini, K. Bollman, H. Sun, and R.S. Poethig Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40 Science 291 2001 2405 2407
    • (2001) Science , vol.291 , pp. 2405-2407
    • Berardini, T.Z.1    Bollman, K.2    Sun, H.3    Poethig, R.S.4
  • 21
    • 0031945523 scopus 로고    scopus 로고
    • Mutation in the Arabidopsis PASTICCINO1 gene, which encodes a new FK506-binding protein-like protein, has a dramatic effect on plant development
    • P. Vittorioso, R. Cowling, J.D. Faure, M. Caboche, and C. Bellini Mutation in the Arabidopsis PASTICCINO1 gene, which encodes a new FK506-binding protein-like protein, has a dramatic effect on plant development Mol Cell Biol 18 1998 3034 3043
    • (1998) Mol Cell Biol , vol.18 , pp. 3034-3043
    • Vittorioso, P.1    Cowling, R.2    Faure, J.D.3    Caboche, M.4    Bellini, C.5
  • 22
    • 0038038605 scopus 로고    scopus 로고
    • Hormonal control of cell proliferation requires PASTICCINO genes
    • Y. Harrar, Y. Bellec, C. Bellini, and J.D. Faure Hormonal control of cell proliferation requires PASTICCINO genes Plant Physiol 132 2003 1217 1227
    • (2003) Plant Physiol , vol.132 , pp. 1217-1227
    • Harrar, Y.1    Bellec, Y.2    Bellini, C.3    Faure, J.D.4
  • 23
    • 0036847334 scopus 로고    scopus 로고
    • Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90
    • T. Kamphausen, J. Fanghanel, D. Neumann, B. Schulz, and J.U. Rahfeld Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90 Plant J 32 2002 263 276
    • (2002) Plant J , vol.32 , pp. 263-276
    • Kamphausen, T.1    Fanghanel, J.2    Neumann, D.3    Schulz, B.4    Rahfeld, J.U.5
  • 24
    • 0842307351 scopus 로고    scopus 로고
    • The ULTRACURVATA2 gene of Arabidopsis encodes an FK506-binding protein involved in auxin and brassinosteroid signaling
    • J.M. Perez-Perez, M.R. Ponce, and J.L. Micol The ULTRACURVATA2 gene of Arabidopsis encodes an FK506-binding protein involved in auxin and brassinosteroid signaling Plant Physiol 134 2004 101 117
    • (2004) Plant Physiol , vol.134 , pp. 101-117
    • Perez-Perez, J.M.1    Ponce, M.R.2    Micol, J.L.3
  • 25
    • 3042762926 scopus 로고    scopus 로고
    • Plant disease resistance protein signaling: NBS-LRR proteins and their partners
    • Y. Belkhadir, R. Subramaniam, and J.L. Dangl Plant disease resistance protein signaling: NBS-LRR proteins and their partners Curr Opin Plant Biol 7 2004 391 399
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 391-399
    • Belkhadir, Y.1    Subramaniam, R.2    Dangl, J.L.3
  • 26
    • 0346965742 scopus 로고    scopus 로고
    • Plant immunity: The origami of receptor activation
    • P. Schulze-Lefert Plant immunity: the origami of receptor activation Curr Biol 14 2004 R22 R24
    • (2004) Curr Biol , vol.14
    • Schulze-Lefert, P.1
  • 30
    • 0042071354 scopus 로고    scopus 로고
    • Role of SGT1 in the regulation of plant R gene signalling
    • P. Muskett, and J. Parker Role of SGT1 in the regulation of plant R gene signalling Microbes Infect 5 2003 969 976
    • (2003) Microbes Infect , vol.5 , pp. 969-976
    • Muskett, P.1    Parker, J.2
  • 31
    • 0038607608 scopus 로고    scopus 로고
    • Complex formation, promiscuity and multi-functionality: Protein interactions in disease-resistance pathways
    • K. Shirasu, and P. Schulze-Lefert Complex formation, promiscuity and multi-functionality: protein interactions in disease-resistance pathways Trends Plant Sci 8 2003 252 258
    • (2003) Trends Plant Sci , vol.8 , pp. 252-258
    • Shirasu, K.1    Schulze-Lefert, P.2
  • 32
    • 0037009437 scopus 로고    scopus 로고
    • Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death
    • P. Moffett, G. Farnham, J. Peart, and D.C. Baulcombe Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death EMBO J 21 2002 4511 4519
    • (2002) EMBO J , vol.21 , pp. 4511-4519
    • Moffett, P.1    Farnham, G.2    Peart, J.3    Baulcombe, D.C.4
  • 33
    • 0036775380 scopus 로고    scopus 로고
    • Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato
    • A. Bendahmane, G. Farnham, P. Moffett, and D.C. Baulcombe Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato Plant J 32 2002 195 204
    • (2002) Plant J , vol.32 , pp. 195-204
    • Bendahmane, A.1    Farnham, G.2    Moffett, P.3    Baulcombe, D.C.4
  • 34
    • 0036914733 scopus 로고    scopus 로고
    • A gain-of-function mutation in an Arabidopsis Toll Interleukin1 receptor-nucleotide binding site-leucine-rich repeat type R gene triggers defense responses and results in enhanced disease resistance
    • Y. Shirano, P. Kachroo, J. Shah, and D.F. Klessig A gain-of-function mutation in an Arabidopsis Toll Interleukin1 receptor-nucleotide binding site-leucine-rich repeat type R gene triggers defense responses and results in enhanced disease resistance Plant Cell 14 2002 3149 3162
    • (2002) Plant Cell , vol.14 , pp. 3149-3162
    • Shirano, Y.1    Kachroo, P.2    Shah, J.3    Klessig, D.F.4
  • 35
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • D. Mackey, Y. Belkhadir, J.M. Alonso, J.R. Ecker, and J.L. Dangl Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance Cell 112 2003 379 389
    • (2003) Cell , vol.112 , pp. 379-389
    • MacKey, D.1    Belkhadir, Y.2    Alonso, J.M.3    Ecker, J.R.4    Dangl, J.L.5
  • 36
    • 6444233160 scopus 로고    scopus 로고
    • Expression of RPS4 in tobacco induces an AvrRps4-independent HR that requires EDS1, SGT1 and HSP90
    • Y. Zhang, S. Dorey, M. Swiderski, and J.D. Jones Expression of RPS4 in tobacco induces an AvrRps4-independent HR that requires EDS1, SGT1 and HSP90 Plant J 40 2004 213 224
    • (2004) Plant J , vol.40 , pp. 213-224
    • Zhang, Y.1    Dorey, S.2    Swiderski, M.3    Jones, J.D.4
  • 37
    • 0037423390 scopus 로고    scopus 로고
    • Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4
    • M.J. Axtell, and B.J. Staskawicz Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4 Cell 112 2003 369 377
    • (2003) Cell , vol.112 , pp. 369-377
    • Axtell, M.J.1    Staskawicz, B.J.2
  • 38
    • 0037155687 scopus 로고    scopus 로고
    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
    • D. Mackey, B.F. Holt, A. Wiig, and J.L. Dangl RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis Cell 108 2002 743 754
    • (2002) Cell , vol.108 , pp. 743-754
    • MacKey, D.1    Holt, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 40
    • 10344257928 scopus 로고    scopus 로고
    • Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream of independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial type III effectors AvrRpt2 or AvrRpm1
    • Y. Belkhadir, Z. Nimchuk, D.A. Hubert, D. Mackey, and J.L. Dangl Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream of independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial type III effectors AvrRpt2 or AvrRpm1 Plant Cell 16 2004 2822 2835
    • (2004) Plant Cell , vol.16 , pp. 2822-2835
    • Belkhadir, Y.1    Nimchuk, Z.2    Hubert, D.A.3    MacKey, D.4    Dangl, J.L.5
  • 42
    • 0033166694 scopus 로고    scopus 로고
    • SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex
    • K. Kitagawa, D. Skowyra, S.J. Elledge, J.W. Harper, and P. Hieter SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex Mol Cell 4 1999 21 33
    • (1999) Mol Cell , vol.4 , pp. 21-33
    • Kitagawa, K.1    Skowyra, D.2    Elledge, S.J.3    Harper, J.W.4    Hieter, P.5
  • 43
    • 0033549777 scopus 로고    scopus 로고
    • Dynamics of disease resistance polymorphism at the Rpm1 locus of Arabidopsis
    • E.A. Stahl, G. Dwyer, R. Mauricio, M. Kreitman, and J. Bergelson Dynamics of disease resistance polymorphism at the Rpm1 locus of Arabidopsis Nature 400 1999 667 671
    • (1999) Nature , vol.400 , pp. 667-671
    • Stahl, E.A.1    Dwyer, G.2    Mauricio, R.3    Kreitman, M.4    Bergelson, J.5
  • 44
    • 1942485896 scopus 로고    scopus 로고
    • The maintenance of extreme amino acid diversity at the disease resistance gene, RPP13, in Arabidopsis thaliana
    • L.E. Rose, P.D. Bittner-Eddy, C.H. Langley, E.B. Holub, R.W. Michelmore, and J.L. Beynon The maintenance of extreme amino acid diversity at the disease resistance gene, RPP13, in Arabidopsis thaliana Genetics 166 2004 1517 1527
    • (2004) Genetics , vol.166 , pp. 1517-1527
    • Rose, L.E.1    Bittner-Eddy, P.D.2    Langley, C.H.3    Holub, E.B.4    Michelmore, R.W.5    Beynon, J.L.6
  • 45
  • 46
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • S.L. Rutherford, and S. Lindquist Hsp90 as a capacitor for morphological evolution Nature 396 1998 336 342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 47
    • 0037228526 scopus 로고    scopus 로고
    • Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution
    • V. Sollars, X. Lu, L. Xiao, X. Wang, M.D. Garfinkel, and D.M. Ruden Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution Nat Genet 33 2003 70 74 The authors identify a new facet of Hsp90 buffering. Using Drosophila melanogaster, they demonstrate that an abnormal eye phenotype is epigenetically inherited, probably through a heritably altered chromatin state.
    • (2003) Nat Genet , vol.33 , pp. 70-74
    • Sollars, V.1    Lu, X.2    Xiao, L.3    Wang, X.4    Garfinkel, M.D.5    Ruden, D.M.6
  • 48
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: Causes, effects and implications of Hsp90-mediated genetic capacitance
    • T.A. Sangster, S. Lindquist, and C. Queitsch Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance Bioessays 26 2004 348 362 A comprehensive review of the evidence for and implications of Hsp90-mediated buffering of genetic variation.
    • (2004) Bioessays , vol.26 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 49
    • 0344824018 scopus 로고    scopus 로고
    • Quantitative trait symmetry independent of Hsp90 buffering: Distinct modes of genetic canalization and developmental stability
    • C.C. Milton, B. Huynh, P. Batterham, S.L. Rutherford, and A.A. Hoffmann Quantitative trait symmetry independent of Hsp90 buffering: distinct modes of genetic canalization and developmental stability Proc Natl Acad Sci USA 100 2003 13396 13401
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13396-13401
    • Milton, C.C.1    Huynh, B.2    Batterham, P.3    Rutherford, S.L.4    Hoffmann, A.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.