메뉴 건너뛰기




Volumn 10, Issue 4, 2003, Pages 250-255

Structural insights into the U-box, a domain associated with multi-ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; MESSENGER RNA PRECURSOR SPLICING FACTOR; PROTEIN PRP19P; UNCLASSIFIED DRUG;

EID: 0037389970     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb906     Document Type: Article
Times cited : (253)

References (36)
  • 1
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 2
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • Cyr, D.M., Hohfeld, J. & Patterson, C. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27, 368-375 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 3
    • 0037154448 scopus 로고    scopus 로고
    • A new gun in town: The U box is a ubiquitin ligase domain
    • Patterson, C. A new gun in town: the U box is a ubiquitin ligase domain. Sci. STKE [online] 〈http://stke.sciencemag.org/cgi/content/full/OC_sigtraus; 2002/116/pe4〉 (2002).
    • (2002) Sci. STKE [Online]
    • Patterson, C.1
  • 4
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M. 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.1
  • 5
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - A common domain in ubiquitination
    • Aravind, L. & Koonin, E.V. The U box is a modified RING finger - a common domain in ubiquitination. Curr. Biol. 10, R132-R134 (2000).
    • (2000) Curr. Biol. , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 6
    • 0027491331 scopus 로고
    • Yeast precursor mRNA processing protein PRP19 associates with the spliceosome concomitant with or just after dissociation of U4 small nuclear RNA
    • Tarn, W.Y., Lee, K.R. & Cheng, S.C. Yeast precursor mRNA processing protein PRP19 associates with the spliceosome concomitant with or just after dissociation of U4 small nuclear RNA. Proc. Natl. Acad. Sci. USA 90, 10821-10825 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10821-10825
    • Tarn, W.Y.1    Lee, K.R.2    Cheng, S.C.3
  • 7
    • 0032771330 scopus 로고    scopus 로고
    • Myb-related fission yeast Cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing
    • McDonald, W.H., Ohl, R., Smelkova, N., Frendewey, D. & Gould, K.L. Myb-related fission yeast Cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing. Mol. Cell. Biol. 19, 5352-5362 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5352-5362
    • McDonald, W.H.1    Ohl, R.2    Smelkova, N.3    Frendewey, D.4    Gould, K.L.5
  • 8
    • 0031901697 scopus 로고    scopus 로고
    • Snt309p, a component of the Prp19p-associated complex that interacts with Prp 19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner as Prp19p
    • Chen, H.R. et al. Snt309p, a component of the Prp19p-associated complex that interacts with Prp19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner as Prp19p. Mol. Cell. Biol. 18, 2196-2204 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2196-2204
    • Chen, H.R.1
  • 9
    • 0036269649 scopus 로고    scopus 로고
    • Characterization of interactions among the Cef1p-Prp19p-associated splicing complex
    • Ohl, M.D. & Gould, K.L. Characterization of interactions among the Cef1p-Prp19p-associated splicing complex. RNA 8, 798-815 (2002).
    • (2002) RNA , vol.8 , pp. 798-815
    • Ohl, M.D.1    Gould, K.L.2
  • 11
    • 0035831429 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the human TFIIH MAT1 subunit: New insights into the RING finger family
    • Gervais, V. et al. Solution structure of the N-terminal domain of the human TFIIH MAT1 subunit: new insights into the RING finger family. J. Biol. Chem. 276, 7457-7464 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 7457-7464
    • Gervais, V.1
  • 12
    • 0035971097 scopus 로고    scopus 로고
    • The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers
    • Hanzawa, H. et al. The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers. J. Biol. Chem. 276, 10185-10190 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 10185-10190
    • Hanzawa, H.1
  • 13
    • 0030959658 scopus 로고    scopus 로고
    • Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster
    • Bellon, S.F., Rodgers, K.K., Schatz, D.G., Coleman, J.E. & Steitz, T.A. Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat. Struct. Biol. 4, 586-591 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5
  • 14
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, R, Jeffrey, P.D. & Pavletich, N.P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, 533-539 (2000).
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, R.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 15
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng, N. et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002).
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 18
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang, L. et al. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 286, 1321-1326 (1999).
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1
  • 19
    • 0035375052 scopus 로고    scopus 로고
    • Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes
    • Pringa, E., Martinez-Noel, G., Muller, U. & Harbers, K. Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes. J. Biol. Chem. 276, 19617-19623 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 19617-19623
    • Pringa, E.1    Martinez-Noel, G.2    Muller, U.3    Harbers, K.4
  • 20
    • 0031901697 scopus 로고    scopus 로고
    • Snt309p, a component of the Prp19p-associated complex that interacts with Prp 19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner as Prp19p
    • Chen, H.R. et al. Snt309p, a component of the Prp19p-associated complex that interacts with Prp19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner as Prp19p. Mol. Cell. Biol. 18, 2196-2204 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2196-2204
    • Chen, H.R.1
  • 21
    • 0024710729 scopus 로고
    • Isolation and characterization of pre-mRNA splicing mutants of Saccharomyces cerevisiae
    • Vijayraghavan, U., Company, M. & Abelson, J. Isolation and characterization of pre-mRNA splicing mutants of Saccharomyces cerevisiae. Genes Dev. 3, 1206-1216 (1989).
    • (1989) Genes Dev. , vol.3 , pp. 1206-1216
    • Vijayraghavan, U.1    Company, M.2    Abelson, J.3
  • 22
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang, J. et al. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276, 42938-42944 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1
  • 23
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata, S., Minami, Y., Minami, M., Chiba, T. & Tanaka, K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2, 1133-1138 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 24
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G.C., Patterson, C., Zhang, W., Younger, J.M. & Cyr, D.M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell. Biol. 3, 100-105 (2001).
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 25
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai, Y. et al. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10, 55-67 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 55-67
    • Imai, Y.1
  • 26
    • 0028365538 scopus 로고
    • Functional association of essential splicing factor(s) with PRP19 in a protein complex
    • Tarn, W.Y. et al. Functional association of essential splicing factor(s) with PRP19 in a protein complex. EMBO J. 13, 2421-2431 (1994).
    • (1994) EMBO J. , vol.13 , pp. 2421-2431
    • Tarn, W.Y.1
  • 28
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (1999).
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 29
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, R, Mumenthaler, C. & Wuthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, R.1    Mumenthaler, C.2    Wuthrich, K.3
  • 30
    • 0004279414 scopus 로고
    • San Francisco, CA.: University of California, San Francisco
    • Pearlman, D.A. et al. AMBER 4.1 (San Francisco, CA.: University of California, San Francisco; 1995).
    • (1995) AMBER 4.1
    • Pearlman, D.A.1
  • 31
    • 0242691764 scopus 로고    scopus 로고
    • High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins
    • Maler, L., Potts, B.C. & Chazin, W.J. High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins. J. Biomol. NMR 13, 233-247 (1999).
    • (1999) J. Biomol. NMR , vol.13 , pp. 233-247
    • Maler, L.1    Potts, B.C.2    Chazin, W.J.3
  • 33
    • 0032520211 scopus 로고    scopus 로고
    • 2+-signal transduction by S100 proteins
    • 2+-signal transduction by S100 proteins. Structure 6, 223-231 (1998).
    • (1998) Structure , vol.6 , pp. 223-231
    • Sastry, M.1
  • 35
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL a program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 36
    • 0030339738 scopus 로고    scopus 로고
    • AQUA PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullman, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486 (1996).
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullman, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.