Structural highlights
Function
[RPN12_SCHPO] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Publication Abstract from PubMed
The ubiquitin proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. We report the crystal structure of Rpn12, a proteasomal PCI- domain containing protein. The structure helps to define a core structural motif for the PCI-domain and identifies potential sites through which Rpn12 might form protein-protein interactions. We demonstrate that mutating residues at one of these sites impairs Rpn12 binding to Rpn10 in vitro and reduces Rpn10 incorporation into proteasomes in vivo.
Structural and functional characterisation of Rpn12 identifies residues required for Rpn10 proteasome incorporation.,Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EO, Lowe ED, Khoudian C, Smith D, Noble ME, Gordon C, Endicott JA Biochem J. 2012 Aug 20. PMID:22906049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EO, Lowe ED, Khoudian C, Smith D, Noble ME, Gordon C, Endicott JA. Structural and functional characterisation of Rpn12 identifies residues required for Rpn10 proteasome incorporation. Biochem J. 2012 Aug 20. PMID:22906049 doi:http://dx.doi.org/10.1042/BJ20120542
