Title |
Structural basis of high‐order oligomerization of the cullin‐3 adaptor SPOP
|
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Published in |
Acta Crystallographica: Section D (International Union of Crystallography - IUCr), August 2013
|
DOI | 10.1107/s0907444913012687 |
Pubmed ID | |
Authors |
Laura K van Geersdaele, Mark A Stead, Christopher M Harrison, Stephen B Carr, Helen J Close, Gareth O Rosbrook, Simon D Connell, Stephanie C Wright |
Abstract |
Protein ubiquitination in eukaryotic cells is mediated by diverse E3 ligase enzymes that each target specific substrates. The cullin E3 ligase complexes are the most abundant class of E3 ligases; they contain various cullin components that serve as scaffolds for interaction with substrate-recruiting adaptor proteins. SPOP is a BTB-domain adaptor of the cullin-3 E3 ligase complexes; it selectively recruits substrates via its N-terminal MATH domain, whereas its BTB domain mediates dimerization and interactions with cullin-3. It has recently been recognized that the high-order oligomerization of SPOP enhances the ubiquitination of substrates. Here, a dimerization interface in the SPOP C-terminus is identified and it is shown that the dimerization interfaces of the BTB domain and of the C-terminus act independently and in tandem to generate high-order SPOP oligomers. The crystal structure of the dimeric SPOP C-terminal domain is reported at 1.5 Å resolution and it is shown that Tyr353 plays a critical role in high-order oligomerization. A model of the high-order SPOP oligomer is presented that depicts a helical organization that could enhance the efficiency of substrate ubiquitination. |
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