CYLD tidies up dishevelled signaling.

Molecular cell ·Vol. 37 ·No. 5 ·2010-03-12 ·Pages 589-90

Komander D

Abstract

An increasing number of cellular signaling pathways utilize protein ubiquitination for activation of signaling cascades. In this issue of Molecular Cell, Maurice and colleagues demonstrate that nondegradative Lys63-linked polyubiquitin chains modulate Dishevelled (Dvl) activity upstream in the Wnt/beta-catenin signaling pathway.

MeSH Terms

Adaptor Proteins, Signal Transducing/genetics,metabolism Animals Carcinoma, Adenoid Cystic/genetics,metabolism,pathology Deubiquitinating Enzyme CYLD Dishevelled Proteins Humans Lysine Mutation Phosphoproteins/genetics,metabolism Protein Processing, Post-Translational Signal Transduction Skin Neoplasms/genetics,metabolism,pathology Transcriptional Activation Tumor Suppressor Proteins/genetics,metabolism Ubiquitination Wnt Proteins/genetics,metabolism Wnt3 Protein beta Catenin/genetics,metabolism

Chemicals

Adaptor Proteins, Signal Transducing CTNNB1 protein, human Dishevelled Proteins Phosphoproteins Tumor Suppressor Proteins Wnt Proteins Wnt3 Protein beta Catenin CYLD protein, human Deubiquitinating Enzyme CYLD Lysine

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Komander David

Medical Research Council Laboratory of Molecular Biology, Protein and Nucleic Acid Chemistry Division, Hills Road, Cambridge CB2 0QH, UK. dk@mrc-lmb.cam.ac.uk

Article Info

Journal

Molecular cell

Abbr.

Mol Cell

ISSN

1097-4164

DOI

10.1016/j.molcel.2010.02.017

dk@mrc-lmb.cam.ac.uk

Published

2010-03-12

Pages

589-90

Language

English

Region

United States

NLM ID

9802571

Subset

Grants

Medical Research Council · MC_U105192732 · United Kingdom

Corrections

CommentOn

PMID: 20227366

External Links

PubMed source DOI: 10.1016/j.molcel.2010.02.017 View journal details

Analysis Services

CYLD tidies up dishevelled signaling.

Contact

WeChat Official Account