| Literature DB >> 22632832 |
Wesley J Errington1, M Qasim Khan, Stephanie A Bueler, John L Rubinstein, Avijit Chakrabartty, Gilbert G Privé.
Abstract
The E3 ligases recruit substrate proteins for targeted ubiquitylation. Recent insights into the mechanisms of ubiquitylation demonstrate that E3 ligases can possess active regulatory properties beyond those of a simple assembly scaffold. Here, we describe the dimeric structure of the E3 ligase adaptor protein SPOP (speckle-type POZ protein) in complex with the N-terminal domain of Cul3 at 2.4 Å resolution. We find that SPOP forms large oligomers that can form heteromeric species with the closely related paralog SPOPL. In combination, SPOP and SPOPL (SPOP-like) form a molecular rheostat that can fine-tune E3 ubiquitin ligase activity by affecting the oligomeric state of the E3 complex. We propose that adaptor protein self-assembly provides a graded level of regulation of the SPOP/Cul3 E3 ligase toward its multiple protein substrates.Entities:
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Year: 2012 PMID： 22632832 DOI： 10.1016/j.str.2012.04.009
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006