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Phosphorylation-dependent Activity of the Deubiquitinase DUBA

Phosphorylation-dependent Activity of the Deubiquitinase DUBA

Oscar W Huang, Xiaolei Ma, JianPing Yin, Jeremy Flinders, Till Maurer, Nobuhiko Kayagaki, Qui Phung, Ivan Bosanac, David Arnott, Vishva M Dixit, Sarah G Hymowitz, Melissa A Starovasnik, Andrea G Cochran

Nat Struct Mol Biol. 2012 Jan 15;19(2):171-5.

PMID: 22245969

Abstract:

Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of interactions involving the phosphate and the C-terminal tail of ubiquitin cause DUBA to fold around its substrate, revealing why phosphorylation is essential for deubiquitinase activity. Phosphoactivation of DUBA represents an unprecedented mode of protease regulation and a clear link between two major cellular signal transduction systems: phosphorylation and ubiquitin modification.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42410922	Ubiquitin Aldehyde			Price

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