期刊
MOLECULAR CELL
卷 36, 期 1, 页码 39-50出版社
CELL PRESS
DOI: 10.1016/j.molcel.2009.09.022
关键词
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资金
- ALSAC (American Lebanese Syrian Associated Charities)
- NIH [R01GM069530, GM070565, P30CA021765]
- Beckman Young InvestigatorAwards
- W.M. Keck Foundation
- Chicago Biomedical Consortium
- Damon Runyon Cancer Research Foundation [DRG 2021-9]
- NCRR [RR-1 5301]
- U.S. DOE, Office of Basic Energy Sciences [W-31-109-ENG-38, 8.2.2]
- HHMI
- NCI [CA92584]
- DOE [DE-AC03-76SF00098, DE-AC02-05CH11231, DE-AC02-98CH 10886]
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination. Here, we present biochemical and structural analyses of the MATH-BTB protein, SPOP. We define a SPOP-binding consensus (SBC) and determine structures revealing recognition of SBCs from the phosphatase Puc, the transcriptional regulator Ci, and the chromatin component MacroH2A. We identify a dimeric SPOP-Cul3 assembly involving a conserved helical structure C-terminal of BTB domains, which we call 3-box due to its facilitating Cul3 binding and its resemblance to F-/SOCS-boxes in other cullin-based E3s. Structural flexibility between the substrate-binding MATH and Cul3-binding BTB/3-box domains potentially allows a SPOP dimer to engage multiple SBCs found within a single substrate, such as Puc. These studies provide a molecular understanding of how MATH-BTB proteins recruit substrates to Cul3 and how their dimerization and conformational variability may facilitate avid interactions with diverse substrates.
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