메뉴 건너뛰기




Volumn 18, Issue 2, 2005, Pages 225-235

The UBA2 domain functions as an intrinsic stabilization signal that protects rad23 from proteasomal degradation

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; MUTANT PROTEIN; PROTEASOME; PROTEIN RAD23; UBIQUITIN ASSOCIATED 2 PROTEIN; UNCLASSIFIED DRUG;

EID: 17044368771     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.03.015     Document Type: Article
Times cited : (94)

References (53)
  • 1
    • 0037518120 scopus 로고    scopus 로고
    • The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions
    • R.C. Aguilar, H.A. Watson, and B. Wendland The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions J. Biol. Chem. 278 2003 10737 10743
    • (2003) J. Biol. Chem. , vol.278 , pp. 10737-10743
    • Aguilar, R.C.1    Watson, H.A.2    Wendland, B.3
  • 2
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • B. Bartel, I. Wunning, and A. Varshavsky The recognition component of the N-end rule pathway EMBO J. 9 1990 3179 3189
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wunning, I.2    Varshavsky, A.3
  • 3
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • W. Baumeister, J. Walz, F. Zuhl, and E. Seemuller The proteasome: paradigm of a self-compartmentalizing protease Cell 92 1998 367 380
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 6
    • 3142712978 scopus 로고    scopus 로고
    • The UV response in Saccharomyces cerevisiae involves the mitogen-activated protein kinase Slt2p
    • B.A. Bryan, G.S. Knapp, L.M. Bowen, and M. Polymenis The UV response in Saccharomyces cerevisiae involves the mitogen-activated protein kinase Slt2p Curr. Microbiol. 49 2004 32 34
    • (2004) Curr. Microbiol. , vol.49 , pp. 32-34
    • Bryan, B.A.1    Knapp, G.S.2    Bowen, L.M.3    Polymenis, M.4
  • 7
    • 0036569345 scopus 로고    scopus 로고
    • From UBA to UBX: New words in the ubiquitin vocabulary
    • A. Buchberger From UBA to UBX: new words in the ubiquitin vocabulary Trends Cell Biol. 12 2002 216 221
    • (2002) Trends Cell Biol. , vol.12 , pp. 216-221
    • Buchberger, A.1
  • 8
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • L. Chen, and K. Madura Rad23 promotes the targeting of proteolytic substrates to the proteasome Mol. Cell. Biol. 22 2002 4902 4913
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 9
    • 0034762028 scopus 로고    scopus 로고
    • Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
    • L. Chen, U. Shinde, T.G. Ortolan, and K. Madura Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly EMBO Rep. 2 2001 933 938
    • (2001) EMBO Rep. , vol.2 , pp. 933-938
    • Chen, L.1    Shinde, U.2    Ortolan, T.G.3    Madura, K.4
  • 10
    • 9744227998 scopus 로고    scopus 로고
    • N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1)
    • X. Chen, Y. Chi, A. Bloecher, R. Aebersold, B.E. Clurman, and J.M. Roberts N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1) Mol. Cell 16 2004 839 847
    • (2004) Mol. Cell , vol.16 , pp. 839-847
    • Chen, X.1    Chi, Y.2    Bloecher, A.3    Aebersold, R.4    Clurman, B.E.5    Roberts, J.M.6
  • 12
    • 0034682502 scopus 로고    scopus 로고
    • Inhibition of proteasomal degradation by the Gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal
    • N.P. Dantuma, S. Heessen, K. Lindsten, M. Jellne, and M.G. Masucci Inhibition of proteasomal degradation by the Gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal Proc. Natl. Acad. Sci. USA 97 2000 8381 8385
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8381-8385
    • Dantuma, N.P.1    Heessen, S.2    Lindsten, K.3    Jellne, M.4    Masucci, M.G.5
  • 13
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • N.P. Dantuma, K. Lindsten, R. Glas, M. Jellne, and M.G. Masucci Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome- dependent proteolysis in living cells Nat. Biotechnol. 18 2000 538 543
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 14
    • 0037010150 scopus 로고    scopus 로고
    • Stabilization signals: A novel regulatory mechanism in the ubiquitin/proteasome system
    • N.P. Dantuma, and M.G. Masucci Stabilization signals: a novel regulatory mechanism in the ubiquitin/proteasome system FEBS Lett. 529 2002 22 26
    • (2002) FEBS Lett. , vol.529 , pp. 22-26
    • Dantuma, N.P.1    Masucci, M.G.2
  • 15
    • 0037079693 scopus 로고    scopus 로고
    • Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination
    • R.T. Elder, X.Q. Song, M. Chen, K.M. Hopkins, H.B. Lieberman, and Y. Zhao Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination Nucleic Acids Res. 30 2002 581 591
    • (2002) Nucleic Acids Res. , vol.30 , pp. 581-591
    • Elder, R.T.1    Song, X.Q.2    Chen, M.3    Hopkins, K.M.4    Lieberman, H.B.5    Zhao, Y.6
  • 16
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • S. Elsasser, D. Chandler-Militello, B. Muller, J. Hanna, and D. Finley Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome J. Biol. Chem. 279 2004 26817 26822
    • (2004) J. Biol. Chem. , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Muller, B.3    Hanna, J.4    Finley, D.5
  • 18
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II
    • A. Ferdous, F. Gonzalez, L. Sun, T. Kodadek, and S.A. Johnston The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II Mol. Cell 7 2001 981 991
    • (2001) Mol. Cell , vol.7 , pp. 981-991
    • Ferdous, A.1    Gonzalez, F.2    Sun, L.3    Kodadek, T.4    Johnston, S.A.5
  • 20
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • F. Gonzalez, A. Delahodde, T. Kodadek, and S.A. Johnston Recruitment of a 19S proteasome subcomplex to an activated promoter Science 296 2002 548 550
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 21
    • 0037472654 scopus 로고    scopus 로고
    • Ubiquitin binding proteins protect ubiquitin conjugates from disassembly
    • R. Hartmann-Petersen, K.B. Hendil, and C. Gordon Ubiquitin binding proteins protect ubiquitin conjugates from disassembly FEBS Lett. 535 2003 77 81
    • (2003) FEBS Lett. , vol.535 , pp. 77-81
    • Hartmann-Petersen, R.1    Hendil, K.B.2    Gordon, C.3
  • 22
    • 0037022303 scopus 로고    scopus 로고
    • Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis
    • S. Heessen, A. Leonchiks, N. Issaeva, A. Sharipo, G. Selivanova, M.G. Masucci, and N.P. Dantuma Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis Proc. Natl. Acad. Sci. USA 99 2002 1532 1537
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1532-1537
    • Heessen, S.1    Leonchiks, A.2    Issaeva, N.3    Sharipo, A.4    Selivanova, G.5    Masucci, M.G.6    Dantuma, N.P.7
  • 24
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • K. Hofmann, and P. Bucher The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway Trends Biochem. Sci. 21 1996 172 173
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 25
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • S. Jentsch, and G. Pyrowolakis Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10 2000 335 342
    • (2000) Trends Cell Biol. , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 26
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • E.S. Johnson, P.C. Ma, I.M. Ota, and A. Varshavsky A proteolytic pathway that recognizes ubiquitin as a degradation signal J. Biol. Chem. 270 1995 17442 17456
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 27
    • 3042764201 scopus 로고    scopus 로고
    • Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
    • I. Kim, K. Mi, and H. Rao Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis Mol. Biol. Cell 15 2004 3357 3365
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3357-3365
    • Kim, I.1    Mi, K.2    Rao, H.3
  • 28
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • M. Koegl, T. Hoppe, S. Schlenker, H.D. Ulrich, T.U. Mayer, and S. Jentsch A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly Cell 96 1999 635 644
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 29
    • 0032879814 scopus 로고    scopus 로고
    • Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae
    • D. Lambertson, L. Chen, and K. Madura Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae Genetics 153 1999 69 79
    • (1999) Genetics , vol.153 , pp. 69-79
    • Lambertson, D.1    Chen, L.2    Madura, K.3
  • 31
    • 0036635969 scopus 로고    scopus 로고
    • The ubiquitin-associated (UBA) domain: On the path from prudence to prurience
    • K. Madura The ubiquitin-associated (UBA) domain: on the path from prudence to prurience Cell Cycle 1 2002 235 244
    • (2002) Cell Cycle , vol.1 , pp. 235-244
    • Madura, K.1
  • 32
    • 0036300780 scopus 로고    scopus 로고
    • Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions
    • T.D. Mueller, and J. Feigon Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions J. Mol. Biol. 319 2002 1243 1255
    • (2002) J. Mol. Biol. , vol.319 , pp. 1243-1255
    • Mueller, T.D.1    Feigon, J.2
  • 34
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • A. Navon, and A.L. Goldberg Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome Mol. Cell 8 2001 1339 1349
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 36
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • S. Prakash, L. Tian, K.S. Ratliff, R.E. Lehotzky, and A. Matouschek An unstructured initiation site is required for efficient proteasome-mediated degradation Nat. Struct. Mol. Biol. 11 2004 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
  • 37
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • S. Raasi, and C.M. Pickart Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains J. Biol. Chem. 278 2003 8951 8959
    • (2003) J. Biol. Chem. , vol.278 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 38
    • 0037023716 scopus 로고    scopus 로고
    • Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23
    • H. Rao, and A. Sastry Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23 J. Biol. Chem. 277 2002 11691 11695
    • (2002) J. Biol. Chem. , vol.277 , pp. 11691-11695
    • Rao, H.1    Sastry, A.2
  • 39
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • M. Rape, T. Hoppe, I. Gorr, M. Kalocay, H. Richly, and S. Jentsch Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone Cell 107 2001 667 677
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 40
    • 0036091848 scopus 로고    scopus 로고
    • Taking a bite: Proteasomal protein processing
    • M. Rape, and S. Jentsch Taking a bite: proteasomal protein processing Nat. Cell Biol. 4 2002 E113 E116
    • (2002) Nat. Cell Biol. , vol.4
    • Rape, M.1    Jentsch, S.2
  • 41
    • 4744372012 scopus 로고    scopus 로고
    • The polyglutamine repeat protein ataxin-1 and its effects on the UbL-UBA protein, A1Up
    • B.E. Riley, Y. Xu, H.Y. Zoghbi, and H.T. Orr The polyglutamine repeat protein ataxin-1 and its effects on the UbL-UBA protein, A1Up J. Biol. Chem. 279 2004 42290 42301
    • (2004) J. Biol. Chem. , vol.279 , pp. 42290-42301
    • Riley, B.E.1    Xu, Y.2    Zoghbi, H.Y.3    Orr, H.T.4
  • 42
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • S.J. Russell, S.H. Reed, W. Huang, E.C. Friedberg, and S.A. Johnston The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair Mol. Cell 3 1999 687 695
    • (1999) Mol. Cell , vol.3 , pp. 687-695
    • Russell, S.J.1    Reed, S.H.2    Huang, W.3    Friedberg, E.C.4    Johnston, S.A.5
  • 43
    • 0036295955 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis
    • Y. Saeki, A. Saitoh, A. Toh-e, and H. Yokosawa Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis Biochem. Biophys. Res. Commun. 293 2002 986 992
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 986-992
    • Saeki, Y.1    Saitoh, A.2    Toh-E, A.3    Yokosawa, H.4
  • 44
    • 0036382885 scopus 로고    scopus 로고
    • Identification of ubiquitin-like protein-binding subunits of the 26S proteasome
    • Y. Saeki, T. Sone, A. Toh-e, and H. Yokosawa Identification of ubiquitin-like protein-binding subunits of the 26S proteasome Biochem. Biophys. Res. Commun. 296 2002 813 819
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 813-819
    • Saeki, Y.1    Sone, T.2    Toh-E, A.3    Yokosawa, H.4
  • 46
    • 0031904016 scopus 로고    scopus 로고
    • A minimal glycine-alanine repeat prevents the interaction of ubiquitinated IκB-α with the proteasome: A new mechanism for selective inhibition of proteolysis
    • A. Sharipo, M. Imreh, A. Leonchiks, S. Imreh, and M.G. Masucci A minimal glycine-alanine repeat prevents the interaction of ubiquitinated IκB-α with the proteasome: a new mechanism for selective inhibition of proteolysis Nat. Med. 4 1998 939 944
    • (1998) Nat. Med. , vol.4 , pp. 939-944
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Imreh, S.4    Masucci, M.G.5
  • 47
    • 0034903337 scopus 로고    scopus 로고
    • In vivo site-directed mutagenesis using oligonucleotides
    • F. Storici, L.K. Lewis, and M.A. Resnick In vivo site-directed mutagenesis using oligonucleotides Nat. Biotechnol. 19 2001 773 776
    • (2001) Nat. Biotechnol. , vol.19 , pp. 773-776
    • Storici, F.1    Lewis, L.K.2    Resnick, M.A.3
  • 49
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • A. Varshavsky The N-end rule: functions, mysteries, uses Proc. Natl. Acad. Sci. USA 93 1996 12142 12149
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 50
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin Chain Receptors Define a Layer of Substrate Selectivity in the Ubiquitin-Proteasome System
    • R. Verma, R. Oania, J. Graumann, and R.J. Deshaies Multiubiquitin Chain Receptors Define a Layer of Substrate Selectivity in the Ubiquitin-Proteasome System Cell 118 2004 99 110
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 51
    • 0345686439 scopus 로고    scopus 로고
    • Ubiquitin recognition by the DNA repair protein hHR23a
    • Q. Wang, A.M. Goh, P.M. Howley, and K.J. Walters Ubiquitin recognition by the DNA repair protein hHR23a Biochemistry 42 2003 13529 13535
    • (2003) Biochemistry , vol.42 , pp. 13529-13535
    • Wang, Q.1    Goh, A.M.2    Howley, P.M.3    Walters, K.J.4
  • 52
    • 0027367944 scopus 로고
    • The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
    • J.F. Watkins, P. Sung, L. Prakash, and S. Prakash The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function Mol. Cell. Biol. 13 1993 7757 7765
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7757-7765
    • Watkins, J.F.1    Sung, P.2    Prakash, L.3    Prakash, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.