Structural highlights
Function
[RPN10_SCHPO] Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19S regulatory particle where it binds to subunits of both the base and lid sub-particles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the VWA domain and characterising the full-length protein by NMR. We demonstrate that the single Ub interacting motif (UIM) of SpRpn10 forms a 1:1 complex with K48-linked diUb, which it binds selectively over monoUb and K63-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid sub-particle, with an affinity comparable to Lys48-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.
The structure of RPN10 and its interactions with polyubiquitin chains and the proteasome subunit RPN12.,Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA J Biol Chem. 2010 Aug 24. PMID:20739285[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wilkinson CR, Ferrell K, Penney M, Wallace M, Dubiel W, Gordon C. Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised. J Biol Chem. 2000 May 19;275(20):15182-92. PMID:10809753
- ↑ Hartmann-Petersen R, Hendil KB, Gordon C. Ubiquitin binding proteins protect ubiquitin conjugates from disassembly. FEBS Lett. 2003 Jan 30;535(1-3):77-81. PMID:12560082
- ↑ Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA. The structure of RPN10 and its interactions with polyubiquitin chains and the proteasome subunit RPN12. J Biol Chem. 2010 Aug 24. PMID:20739285 doi:10.1074/jbc.M110.134510
