The E3 ligase CHIP: Insights into its structure and regulation

74Citations
Citations of this article
112Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

The carboxy-terminus of Hsc70 interacting protein (CHIP) is a cochaperone E3 ligase containing three tandem repeats of tetratricopeptide (TPR) motifs and a C-terminal U-box domain separated by a charged coiled-coil region. CHIP is known to function as a central quality control E3 ligase and regulates several proteins involved in a myriad of physiological and pathological processes. Recent studies have highlighted varied regulatory mechanisms operating on the activity of CHIP which is crucial for cellular homeostasis. In this review article, we give a concise account of our current knowledge on the biochemistry and regulation of CHIP. © 2014 Indranil Paul and Mrinal K. Ghosh.

Cite

CITATION STYLE

APA

Paul, I., & Ghosh, M. K. (2014). The E3 ligase CHIP: Insights into its structure and regulation. BioMed Research International. Hindawi Publishing Corporation. https://doi.org/10.1155/2014/918183

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free