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Volumn 41, Issue , 2005, Pages 31-48

Proteasomes

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA;

EID: 27144503392     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/bse0410031     Document Type: Review
Times cited : (49)

References (48)
  • 2
    • 0037712997 scopus 로고    scopus 로고
    • The ubiquitin/26 S proteasome pathway, the complex last chapter in life of many plant proteins
    • Viestra, R.D. (2003) The ubiquitin/26 S proteasome pathway, the complex last chapter in life of many plant proteins. Trends Plant Sci. 8, 135-142
    • (2003) Trends Plant Sci. , vol.8 , pp. 135-142
    • Viestra, R.D.1
  • 3
    • 0032426798 scopus 로고    scopus 로고
    • Intracellular proteinases of invertebrates: Calcium-dependent and proteasome/ubiquitin-dependent systems
    • Mykles, D.L. (1998) Intracellular proteinases of invertebrates: calcium-dependent and proteasome/ubiquitin-dependent systems. Int. Rev. Cytol. 184, 157-289
    • (1998) Int. Rev. Cytol. , vol.184 , pp. 157-289
    • Mykles, D.L.1
  • 4
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M.H. & Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 5
    • 0042313977 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26 S proteasome
    • Imai, J., Maruya, M., Yashiroda, H., Yahara, I. & Tanaka, K. (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26 S proteasome. EMBO J. 22, 3557-3567
    • (2003) EMBO J. , vol.22 , pp. 3557-3567
    • Imai, J.1    Maruya, M.2    Yashiroda, H.3    Yahara, I.4    Tanaka, K.5
  • 6
    • 17644421410 scopus 로고    scopus 로고
    • Proteasomal ATPase-associated factor I negatively regulates proteasome activity by interacting with proteasomal ATPases
    • Park, Y., Hwang, Y.-P., Lee, J.-S., Seo, S.-H., Yoon, S.K. & Yoon, J.-B. (2005) Proteasomal ATPase-associated factor I negatively regulates proteasome activity by interacting with proteasomal ATPases. Mol. Cell. Biol. 25, 3842-3853
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3842-3853
    • Park, Y.1    Hwang, Y.-P.2    Lee, J.-S.3    Seo, S.-H.4    Yoon, S.K.5    Yoon, J.-B.6
  • 7
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20 S and 26 S proteasomes
    • Coux, O., Tanaka, K. & Goldberg, A.L. (1996) Structure and functions of the 20 S and 26 S proteasomes. Annu. Rev. Biochem. 65, 801-847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 8
    • 0032867676 scopus 로고    scopus 로고
    • The 26 S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., Zwickl, P. & Baumeister, W. (1999) The 26 S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 9
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel, S. & Latterich, M. (1998) The AAA team: related ATPases with diverse functions. Trend Cell Biol. 8, 65-71
    • (1998) Trend Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 11
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richy, H., Rape, M., Braun, S., Rumpf, S., Hoege, C. & Jentsch, S. (2005) A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84
    • (2005) Cell , vol.120 , pp. 73-84
    • Richy, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 12
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome-system
    • Verma, R., Oania, R., Graumann, J. & Deshaies, R.J. (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome-system. Cell 118, 99-110
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 13
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recogniton of ornithine decarboxylase, a ubiquitin-independent substrate
    • Zhang,M., Pickart, C.M. & Coffino, P. (2003) Determinants of proteasome recogniton of ornithine decarboxylase, a ubiquitin-independent substrate. EMBO J. 22, 1488-1496
    • (2003) EMBO J. , vol.22 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Coffino, P.3
  • 14
    • 0142250763 scopus 로고    scopus 로고
    • Proteasome degradation: Enter the substrate
    • Förster, A. & Hill, C.P. (2003) Proteasome degradation: enter the substrate. Trends Cell Biol. 13, 550-553
    • (2003) Trends Cell Biol. , vol.13 , pp. 550-553
    • Förster, A.1    Hill, C.P.2
  • 15
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory PAN serves multiple functions in protein degradation
    • Benaroudj, N., Zwickl, P., Seemüller, E., Baumeister, W. & Goldberg, A.L. (2003) ATP hydrolysis by the proteasome regulatory PAN serves multiple functions in protein degradation. Mol. Cell 11, 69-78
    • (2003) Mol. Cell , vol.11 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seemüller, E.3    Baumeister, W.4    Goldberg, A.L.5
  • 16
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • Prakash, S., Tian, L., Ratliff, K.S., Lehotzky, R.E. & Matouschek, A. (2004) An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol. Biol. 11, 830-837
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 18
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Rubin, D.M., Glickman, M.H., Larsen, C.N., Dhruvakumar, S., & Finley, D. (1998) Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17, 4909-4919
    • (1998) EMBO J. , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 19
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T. & Cohen R.E. (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature (London) 419, 403-407
    • (2002) Nature (London) , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 20
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik, A.Y. & Hochstrasser, M. (2004) Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 1695, 189-207
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 23
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • Köhler, A., Cascio, P., Legett, D.S., Woo, K.M., Goldberg, A.L. & Finley, D. (2001) The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7, 1143-1152
    • (2001) Mol. Cell , vol.7 , pp. 1143-1152
    • Köhler, A.1    Cascio, P.2    Legett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 25
    • 3342972911 scopus 로고    scopus 로고
    • Two substrate association with the 20 S proteasome at single molecule level
    • Hutschenreiter, S., Tinazli, A., Model, K. & Tampé, R. (2004) Two substrate association with the 20 S proteasome at single molecule level. EMBO J. 23, 2488-2497
    • (2004) EMBO J. , vol.23 , pp. 2488-2497
    • Hutschenreiter, S.1    Tinazli, A.2    Model, K.3    Tampé, R.4
  • 27
    • 0036300868 scopus 로고    scopus 로고
    • Assessment of proteasomal cleavage probabilities from kinetic analysis of time-dependent product formation
    • Peters, B., Janek, K., Kuckelkorn, U. & Holzhütter, H.G. (2002) Assessment of proteasomal cleavage probabilities from kinetic analysis of time-dependent product formation. J. Mol. Biol. 318, 847-862
    • (2002) J. Mol. Biol. , vol.318 , pp. 847-862
    • Peters, B.1    Janek, K.2    Kuckelkorn, U.3    Holzhütter, H.G.4
  • 28
    • 9644302406 scopus 로고    scopus 로고
    • Productive RUPture: Activation of transcription factors by proteasomal processing
    • Rape, M. & Jentsch, S. (2004) Productive RUPture: activation of transcription factors by proteasomal processing. Biochim. Biophys. Acta 1695, 209-213
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 209-213
    • Rape, M.1    Jentsch, S.2
  • 30
    • 0035853037 scopus 로고    scopus 로고
    • RPN4 is a ligand, substrate, and transcriptional reglator of the 26 S proteasomes: A negative feedback circuit
    • Xie, Y. & Varshavsky, A. (2001) RPN4 is a ligand, substrate, and transcriptional reglator of the 26 S proteasomes: a negative feedback circuit. Proc. Natl. Acad. Sci. U.S.A. 98, 3056-3061
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3056-3061
    • Xie, Y.1    Varshavsky, A.2
  • 32
    • 3242714839 scopus 로고    scopus 로고
    • The ultimate nanoscale mincer: Assembly, structure and active sites of the 20 S proteasomes core
    • Heinemeyer, W., Ramos, P.C. & Dohmen, R.J. (2004) The ultimate nanoscale mincer: assembly, structure and active sites of the 20 S proteasomes core. Cell. Mol. Life Sci. 61, 1562-1578
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1562-1578
    • Heinemeyer, W.1    Ramos, P.C.2    Dohmen, R.J.3
  • 33
    • 21544475903 scopus 로고    scopus 로고
    • IFNγ-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink, S., Ludwig, D., Kloetzel, P.-M. & Krüger, E. (2005) IFNγ-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc. Natl. Acad. Sci. U.S.A. 102, 9241-9246
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.-M.3    Krüger, E.4
  • 34
    • 0842277344 scopus 로고    scopus 로고
    • The components of the proteasome system and their role in MHC class I antigen processing
    • Krüger, E., Kuckelkorn, U., Sijts, A. & Kloetzel, P.-M. (2003) The components of the proteasome system and their role in MHC class I antigen processing. Rev. Physiol. Biochem. Pharmacol. 148, 81-104
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.148 , pp. 81-104
    • Krüger, E.1    Kuckelkorn, U.2    Sijts, A.3    Kloetzel, P.-M.4
  • 38
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-γ and contribution to ATP-dependent proteolysis
    • Tanahashi, N., Murakami, Y., Minami, Y., Shimbara, N., Hendil, K.B. & Tanaka, K. (2000) Hybrid proteasomes. Induction by interferon-γ and contribution to ATP-dependent proteolysis. J. Biol. Chem. 275, 14336-14345
    • (2000) J. Biol. Chem. , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 39
    • 0037013955 scopus 로고    scopus 로고
    • Properties of the hybrid form of the 26S proteasomes containing both 19S and PA28 complexes
    • Cascio, P., Call, M., Petre, B.M., Walz, T. & Goldberg, A.L. (2002) Properties of the hybrid form of the 26S proteasomes containing both 19S and PA28 complexes. EMBO J. 21, 2636-2645
    • (2002) EMBO J. , vol.21 , pp. 2636-2645
    • Cascio, P.1    Call, M.2    Petre, B.M.3    Walz, T.4    Goldberg, A.L.5
  • 41
    • 0037834898 scopus 로고    scopus 로고
    • Ubiquitin-independent proteolytic functions of the proteasome
    • Orlowski, M. & Wilk, S. (2003) Ubiquitin-independent proteolytic functions of the proteasome. Arch. Biochem. Biophys. 415, 1-5
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 1-5
    • Orlowski, M.1    Wilk, S.2
  • 42
    • 1542375145 scopus 로고    scopus 로고
    • Non-traditional roles of ubiquitin-proteasome system in fertilization and gametogenesis
    • Sakai, N., Sawada, M.T. & Sawada, H. (2004) Non-traditional roles of ubiquitin-proteasome system in fertilization and gametogenesis. Int. J. Biochem. Cell Biol. 36, 776-784
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 776-784
    • Sakai, N.1    Sawada, M.T.2    Sawada, H.3
  • 43
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • Rechsteiner, M. & Hill, C.P. (2005) Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15, 27-33
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 44
    • 2142715911 scopus 로고    scopus 로고
    • Purification procedures determine the proteasome activation properties of REGγ (PA28γ)
    • Gao, X., Li, J., Pratt, G., Wilk, S. & Rechsteiner, M. (2004) Purification procedures determine the proteasome activation properties of REGγ (PA28γ). Arch. Biochem. Biophys. 425, 158-164
    • (2004) Arch. Biochem. Biophys. , vol.425 , pp. 158-164
    • Gao, X.1    Li, J.2    Pratt, G.3    Wilk, S.4    Rechsteiner, M.5
  • 45
    • 0035928749 scopus 로고    scopus 로고
    • Protein stability: The COP9 signalosome gets in on the act
    • Seeger, M., Gordon, C. & Dubiel, W. (2001) Protein stability: the COP9 signalosome gets in on the act. Curr. Biol. 11, R643-R646
    • (2001) Curr. Biol. , vol.11
    • Seeger, M.1    Gordon, C.2    Dubiel, W.3
  • 46
    • 0035841193 scopus 로고    scopus 로고
    • Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome
    • Cagney, G., Uetz, P. & Fields, S. (2001) Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome. Physiol. Genomics 7, 27-34
    • (2001) Physiol. Genomics , vol.7 , pp. 27-34
    • Cagney, G.1    Uetz, P.2    Fields, S.3
  • 48
    • 11144225834 scopus 로고    scopus 로고
    • Characterization of mammalian Ecm-29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles
    • Gorbea, C., Goellner, G.M., Teter, K., Holmes, R.K. & Rechsteiner, M. (2004) Characterization of mammalian Ecm-29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles. J. Biol. Chem. 279, 54849-54861
    • (2004) J. Biol. Chem. , vol.279 , pp. 54849-54861
    • Gorbea, C.1    Goellner, G.M.2    Teter, K.3    Holmes, R.K.4    Rechsteiner, M.5


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