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Article

The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates.

The Journal of biological chemistry - 26 Feb 2010

Ogunjimi Abiodun A, Wiesner Silke, Briant Douglas J, Varelas Xaralabos, Sicheri Frank, Forman-Kay Julie, Wrana Jeffrey L

Abstract excerpt

Mono- and polyubiquitylation of proteins are key steps in a wide range of biological processes. However, the molecular mechanisms that mediate these different events are poorly understood. Here, we employed NMR spectroscopy to map a non-covalent ubiquitin binding surface (UBS) on the Smurf ubiquitin ligase HECT domain. Analysis of mutants of the HECT UBS reveal that interfering with the UBS surface blocked...

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Identifiers

PMID: 20026602
DOI: 10.1074/jbc.M109.044537
PMCID: PMC2825426

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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