Selective protein degradation in cell signalling

Seminars in Cell & Developmental Biology
Han LiuMichael J Clague

Abstract

A variety of post-translational modifications such as phosphorylation, acetylation and ubiquitylation transduce cellular signals, which culminate in changes in gene transcription. In this article we examine the ways in which selective protein degradation provides an extra dimension to the regulation of such signalling cascades. We discuss (i) how both lysosomal and proteasomal systems are used to attenuate kinase and rho family GTPase signalling, thereby coupling activation with degradation, (ii) signal propagation contingent upon the selective degradation of inhibitory components, exemplified by the degradation of IκB to activate NF-κB signalling, and (iii) tonic suppression of signalling pathways by turnover of the transcription factors β-catenin and p53.

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Citations

May 15, 2013·Annual Review of Genomics and Human Genetics·Maria Antonietta De MatteisCathal Wilson
Jul 8, 2015·The Journal of Cell Biology·Christoph GerhardtUlrich Rüther
Oct 8, 2016·Nature Communications·Rebecca L EcclesOliver Rocks
Jan 9, 2017·The FEBS Journal·Michael J Clague, Sylvie Urbé
Mar 26, 2021·Synthetic Biology·Brianna JayanthiLaura Segatori

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