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Article

A Tunable Brake for HECT Ubiquitin Ligases.

Molecular cell - 4 May 2017

Chen Zan, Jiang Hanjie, Xu Wei, Li Xiaoguang, Dempsey Daniel R, Zhang Xiangbin, Devreotes Peter, Wolberger Cynthia, Amzel L Mario, Gabelli Sandra B, Cole Philip A

Abstract excerpt

The HECT E3 ligases ubiquitinate numerous transcription factors and signaling molecules, and their activity must be tightly controlled to prevent cancer, immune disorders, and other diseases. In this study, we have found unexpectedly that peptide linkers tethering WW domains in several HECT family members are key regulatory elements of their catalytic activities. Biochemical, structural, and cellular analyses...

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Share to Protein Domains
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endosomal Sorting Complexes Required for Transport

Share to Enzyme Stability

Share to Nedd4 Ubiquitin Protein Ligases

Share to Protein Processing, Post-Translational

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Source

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Identifiers

PMID: 28475870
DOI: 10.1016/j.molcel.2017.03.020
PMCID: PMC5489419

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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