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• W2187443601 abstract "Sgt1 is an adaptor protein implicated in a variety ofprocesses, including formation of the kinetochore complexin yeast, and regulation of innate immunity systems inplants and animals. Sgt1 has been found to associate withSCF E3 ubiquitin ligases, the CBF3 kinetochore complex,plant R proteins and related animal Nod-like receptors,and with the Hsp90 molecular chaperone. We have deter-mined the crystal structure of the core Hsp90–Sgt1 com-plex, revealing a distinct site of interaction on the Hsp90N-terminal domain. Using the structure, we developedmutations in Sgt1 interfacial residues, which specificallyabrogate interaction with Hsp90, and disrupt Sgt1-depen-dent functions in vivo, in plants and yeast. We show thatSgt1 bridges the Hsp90 molecular chaperone system to thesubstrate-specific arm of SCF ubiquitin ligase complexes,suggesting a role in SCF assembly and regulation, andproviding multiple complementary routes for ubiquitina-tion of Hsp90 client proteins.The EMBO Journal (2008) 27, 2789–2798. doi:10.1038/emboj.2008.190; Published online 25 September 2008Subject Categories: proteins; structural biologyKeywords: complex assembly; crystal structure; molecularchaperone; protein–protein interactions; ubiquitin ligase" @default.
• W2187443601 created "2016-06-24" @default.
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• W2187443601 date "2008-01-01" @default.
• W2187443601 modified "2023-09-27" @default.
• W2187443601 title "Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited.Thislicensedoesnot permit commercial exploitation or the creation of derivative works without specific permission." @default.
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