The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome

Molecular Biology of the Cell

Volumn 14, Issue 9, 2003, Pages 3868-3875

  Kleijnen, Maurits F ^a   Alarcón, Rodolfo M ^a   Howley, Peter M ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; PRESENILIN 1; PROTEASOME; PROTEIN HPLIC 2; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

CELL CYCLE PROTEINS; CLONING, MOLECULAR; CYSTEINE ENDOPEPTIDASES; HELA CELLS; HUMANS; MULTIENZYME COMPLEXES; PRECIPITIN TESTS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; TUMOR SUPPRESSOR PROTEIN P53; UBIQUITINS;

EID: 0141632772     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-11-0766     Document Type: Article

References (43)

1. Baumeister, W., Walz, J., Zuhl, F., and Seemuller, E. (1998). The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380.
2. Bedford, F.K., Kittler, J.T., Muller, E., Thomas, P., Uren, J.M., Merlo, D., Wisden, W., Triller, A., Smart, T.G., and Moss, S.J. (2001). GABA(A) receptor cell surface number and subunit stability are regulated by the ubiquitin-like protein Plic-1. Nat. Neurosci. 4, 908-916.
3. Bertolaet, B.L., Clarke, D.J., Wolff, M., Watson, M.H., Henze, M., Divita, G., and Reed, S.I. (2001a). UBA domains mediate protein-protein interactions between two DNA damage-inducible proteins. J. Mol. Biol. 313, 955-963.
4. Bertolaet, B.L., Clarke, D.J., Wolff, M., Watson, M.H., Henze, M., Divita, G., and Reed, S.I. (2001b). UBA domains of DNA damage-inducible proteins interact with ubiquitin. Nat. Struct. Biol. 8, 417-422.
5. Bogyo, M., Shin, S., McMaster, J.S., and Ploegh, H.L. (1998). Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes. Chem. Biol. 5, 307-320.
6. Chen, L., and Madura, K. (2002). Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol. Cell. Biol. 22, 4902-4913.
7. Chen, L., Shinde, U., Ortolan, T.G., and Madura, K. (2001). Ubiquitin-associated (uba) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly. EMBO Rep. 2, 1-6.
8. Ciechanover, A. (1998). The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17, 7151-7160.
9. Clarke, D.J., Mondesert, G., Segal, M., Bertolaet, B.L., Jensen, S., Wolff, M., Henze, M., and Reed, S.I. (2001). Dosage suppressors of pdsl implicate ubiquitin-associated domains in checkpoint control. Mol. Cell. Biol. 21, 1997-2007.
10. Coux, O., Tanaka, K., and Goldberg, A.L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
11. Dieckmann, T., Withers-Ward, E.S., Jarosinski, M.A., Liu, C.F., Chen, I.S., and Feigon, J. (1998). Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr. Nat. Struct. Biol. 5, 1042-1047.
12. Elsasser, S., Gali, R., Schwickart, M., Larsen, C., Leggett, D.S., Mueller, B., Feng, M., Tuebing, F., Dittmar, G., and Finley, D. (2002). Proteasome subunit Rpnl binds ubiquitin-like protein domains. Nat. Cell Biol. 4, 725-730.
13. Funakoshi, M., Sasaki, T., Nishimoto, T., and Kobayashi, H. (2002). Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. USA 99, 745-750.
14. Henry, L., Baz, A., Chateau, M.-T., Caravano, R., Scherrer, K., and Bureau, J.P. (1997). Proteasome (prosome) subunit variations during the differentiation of myeloid U937 cells. Anal. Cell. Pathol. 15, 131-144.
15. Hershko, A., and Ciechanover, A. (1998). The ubiquitin system. Annu. Rev. Biochem. 1998, 425-479.
16. Hiyama, H., Yokoi, M., Masutani, C., Sugasawa, K., Maekawa, T., Tanaka, K., Hoeijmakers, J.H.J., and Hanaoka, F. (1999). Interaction of hHR23 with S5a. J. Biol. Chem. 274, 28019-28025.
17. Hochstrasser, M. (2000). Evolution and function of ubiquitin-like protein-conjugation systems. Nat. Cell Biol. 2, E153-E157.
18. Hofmann, K., and Bucher, P. (1996). The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 21, 172-173.
19. Jentsch, S., and Pyrowolakis, G. (2000). Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335-342.
20. Kaye, F.J., Modi, S., Ivanovska, I., Koonin, E.V., Thress, K., Kubo, A., Kornbluth, S., and Rose, M.D. (2000). A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett. 467, 348-355.
21. Kleijnen, M.F., Shih, A.H., Zhou, P., Kumar, S., Soccio, R.E., Kedersha, N.L., Gill, G., and Howley, P.M. (2000). The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. Mol. Cell 6, 409-419.
22. Leggett, D.S., Hanna, J., Borodovsky, A., Crossas, B., Schmidt, M., Baker, R.T., Walz, T., Ploegh, H., and Finley, D. (2002). Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495-507.
23. Luders, J., Demand, J., and Hohfeld, J, (2000). The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275, 4613-4617.
24. Mah, A.L., Perry, G., Smith, M.A., and Monteiro, M.J. (2000). Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation. J. Cell Biol. 151, 847-862.
25. Miao, F., Bouziane, M., Dammann, R., Masutani, C., Hanaoka, F., Pfeifer, G., and O'Connor, T.R. (2000). 3-Methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteins proteins. J. Biol. Chem. 275, 28433-28438.
26. Mueller, T.D., and Feigon, J. (2002). Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. J. Mol. Biol. 319, 1243-1255.
27. Ortolan, T.G., Tongaonkar, P., Lambertson, D., Chen, L., Schauber, C., and Madura, K. (2000). The DNA repair protein Rad23 is a negative regulator of multi-ubiquitin chain assembly. Nat. Cell Biol. 2, 601-608.
28. Pickart, C.M. (2001). Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533.
29. Rao, H., and Sastry, A. (2002). Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J. Biol. Chem. 277, 11691-11695.
30. Schauber, C., Chen, L., Tongaonkar, P., Vega, I., Lambertson, D., Potts, W., and Madura, K. (1998). Rad23 links DNA repair to the ubiquitin/proteasome pathway. Nature 391, 715-718.
31. Scheffner, M., Huibregtse, J.M., Vierstra, R.D., and Howley, P.M. (1993). The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505.
32. Scheffner, M., Werness, B.A., Huibregtse, J.M., Levine, A.J., and Howley, P.M. (1990). The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63, 1129-1136.
33. Silva Pereira, I., Bey, F., and Scherrer, K. (1992). Two mRNAs exist for the Hs PROS-30 gene encoding a component of human prosomes. Gene 120, 235-242.
34. Tongaonkar, P., Chen, L., Lambertson, D., Ko, B., and Madura, K. (2000). Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome. Mol. Cell. Biol. 20, 4691-4698.
35. Vadlamudi, R.K., Joung, I., Strominger, J.L., and Shin, J. (1996). p62, a phosphotyrosine-independent ligand of the SH2 domain of p561ck, belongs to a new class of ubiquitin-binding proteins. J. Biol. Chem. 271, 20235-20237.
36. Verma, R., Chen, S., Feldman, R., Schieltz, D., Yates, J., Dohmen, J., and Deshaies, R.J. (2000). Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11, 3425-3439.
37. Voges, D., Zwickl, P., and Baumeister, W. (1999). The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068.
38. Walters, K.J., Kleijnen, M.F., Goh, A.M., Wagner, G., and Howley, P.M. (2002). Structural studies of the interaction between ubiquitin family proteins and the proteasome subunit S5a. Biochemistry 41, 1767-1777.
39. Wilkinson, C.R., Seeger, M., Hartmann-Petersen, R., Stone, M., Wallace, M., Semple, C., and Gordon, C. (2001). Proteins containing the UBA domain are able to bind to multi-ubiquitin chains. Nat. Cell Biol. 3, 939-943.
40. Withers-Ward, E.S., et al. (1997). Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair. J. Virol. 71, 9732-9742.
41. Withers-Ward, E.S., Mueller, T.D., Chen, I.S., and Feigon, J. (2000). Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr. Biochemistry 39, 14103-14112.
42. Xie, Y., and Varshavsky, A. (2000). Physical association of ubiquitin ligases and the 26S proteasome. Proc. Natl. Acad. Sci. USA 97, 2497-2502.
43. Xie, Y., and Varshavsky, A. (2002). UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat. Cell Biol. 4, 1003-1007.