Ecm29 Fulfils Quality Control Functions in Proteasome Assembly

Molecular Cell

Volumn 38, Issue 6, 2010, Pages 879-888

  Lehmann, Andrea ^a   Niewienda, Agathe ^a   Jechow, Katharina ^a   Janek, Katharina ^a   Enenkel, Cordula ^a  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

PROTEINS

Indexed keywords

ECM29 PROTEIN, S CEREVISIAE; PROTEASOME; PROTEIN SUBUNIT; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; ENZYMOLOGY; GENETICS; METABOLISM; PHYSIOLOGY; SACCHAROMYCES CEREVISIAE;

PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN SUBUNITS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

MLCS; MLOWN;

EID: 77955503621     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2010.06.016     Document Type: Article

References (29)

1. Babbitt, S.E., Kiss, A., Deffenbaugh, A.E., Chang, Y.H., Bailly, E., Erdjument-Bromage, H., Tempst, P., Buranda, T., Sklar, L.A., Baumler, J., et al. ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle. Cell 121 (2005), 553–565.
2. Besche, H.C., Peth, A., Goldberg, A.L., Getting to first base in proteasome assembly. Cell 138 (2009), 25–28.
3. Chen, P., Hochstrasser, M., Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86 (1996), 961–972.
4. Fehlker, M., Wendler, P., Lehmann, A., Enenkel, C., Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 4 (2003), 959–963.
5. Goldberg, A.L., Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans. 35 (2007), 12–17.
6. Groll, M., Bajorek, M., Köhler, A., Moroder, L., Rubin, D.M., Huber, R., Glickman, M.H., Finley, D., A gated channel into the proteasome core particle. Nat. Struct. Biol. 7 (2000), 1062–1067.
7. Hershko, A., Ciechanover, A., The ubiquitin system. Annu. Rev. Biochem. 67 (1998), 425–479.
8. Isono, E., Nishihara, K., Saeki, Y., Yashiroda, H., Kamata, N., Ge, L., Ueda, T., Kikuchi, Y., Tanaka, K., Nakano, A., Toh-e, A., The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome. Mol. Biol. Cell 18 (2007), 569–580.
9. Iwanczyk, J., Sadre-Bazzaz, K., Ferrell, K., Kondrashkina, E., Formosa, T., Hill, C.P., Ortega, J., Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes. J. Mol. Biol. 363 (2006), 648–659.
10. Kajava, A.V., Gorbea, C., Ortega, J., Rechsteiner, M., Steven, A.C., New HEAT-like repeat motifs in proteins regulating proteasome structure and function. J. Struct. Biol. 146 (2004), 425–430.
11. Kleijnen, M.F., Kirkpatrick, D.S., Gygi, S.P., The ubiquitin-proteasome system regulates membrane fusion of yeast vacuoles. EMBO J. 26 (2007), 275–287.
12. Kleijnen, M.F., Roelofs, J., Park, S., Hathaway, N.A., Glickman, M., King, R.W., Finley, D., Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. Nat. Struct. Mol. Biol. 14 (2007), 1180–1188.
13. Kriegenburg, F., Seeger, M., Saeki, Y., Tanaka, K., Lauridsen, A.M., Hartmann-Petersen, R., Hendil, K.B., Mammalian 26S proteasomes remain intact during protein degradation. Cell 135 (2008), 355–365.
14. Kusmierczyk, A.R., Hochstrasser, M., Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis. Biol. Chem. 389 (2008), 1143–1151.
15. Le Tallec, B., Barrault, M.B., Courbeyrette, R., Guérois, R., Marsolier-Kergoat, M.C., Peyroche, A., 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol. Cell 27 (2007), 660–674.
16. Leggett, D.S., Hanna, J., Borodovsky, A., Crosas, B., Schmidt, M., Baker, R.T., Walz, T., Ploegh, H., Finley, D., Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10 (2002), 495–507.
17. Lehmann, A., Janek, K., Braun, B., Kloetzel, P.M., Enenkel, C., 20 S proteasomes are imported as precursor complexes into the nucleus of yeast. J. Mol. Biol. 317 (2002), 401–413.
18. Lehmann, A., Jechow, K., Enenkel, C., Blm10 binds to pre-activated proteasome core particles with open gate conformation. EMBO Rep. 9 (2008), 1237–1243.
19. Li, X., Kusmierczyk, A.R., Wong, P., Emili, A., Hochstrasser, M., beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint. EMBO J. 26 (2007), 2339–2349.
20. Marques, A.J., Glanemann, C., Ramos, P.C., Dohmen, R.J., The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation. J. Biol. Chem. 282 (2007), 34869–34876.
21. Metzger, M.B., Michaelis, S., Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol. Biol. Cell 20 (2009), 1006–1019.
22. Murata, S., Yashiroda, H., Tanaka, K., Molecular mechanisms of proteasome assembly. Nat. Rev. Mol. Cell Biol. 10 (2009), 104–115.
23. Osmulski, P.A., Hochstrasser, M., Gaczynska, M., A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel. Structure 17 (2009), 1137–1147.
24. Ramos, P.C., Dohmen, R.J., PACemakers of proteasome core particle assembly. Structure 16 (2008), 1296–1304.
25. Ramos, P.C., Höckendorff, J., Johnson, E.S., Varshavsky, A., Dohmen, R.J., Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92 (1998), 489–499.
26. Schmidt, M., Haas, W., Crosas, B., Santamaria, P.G., Gygi, S.P., Walz, T., Finley, D., The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat. Struct. Mol. Biol. 12 (2005), 294–303.
27. Schmidtke, G., Kraft, R., Kostka, S., Henklein, P., Frömmel, C., Löwe, J., Huber, R., Kloetzel, P.M., Schmidt, M., Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis. EMBO J. 15 (1996), 6887–6898.
28. Tanaka, K., The proteasome: overview of structure and functions. Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. 85 (2009), 12–36.
29. Xie, Y., Varshavsky, A., RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proc. Natl. Acad. Sci. USA 98 (2001), 3056–3061.