A CHIPotle in physiology and disease

Indranil Paul; Mrinal K Ghosh

doi:10.1016/j.biocel.2014.10.027

A CHIPotle in physiology and disease

Int J Biochem Cell Biol. 2015 Jan:58:37-52. doi: 10.1016/j.biocel.2014.10.027. Epub 2014 Nov 1.

Authors

Indranil Paul¹, Mrinal K Ghosh²

Affiliations

¹ Cancer Biology and Inflammatory Disorder Division, Council of Scientific and Industrial Research - Indian Institute of Chemical Biology (CSIR-IICB), 4, Raja S.C. Mullick Road, Kolkata 700032, India.
² Cancer Biology and Inflammatory Disorder Division, Council of Scientific and Industrial Research - Indian Institute of Chemical Biology (CSIR-IICB), 4, Raja S.C. Mullick Road, Kolkata 700032, India. Electronic address: mrinal.res@gmail.com.

PMID: 25448416
DOI: 10.1016/j.biocel.2014.10.027

Abstract

The carboxy-terminus of Hsc70 interacting protein (CHIP) is known to function as a chaperone associated E3 ligase for several proteins and regulates a variety of physiological processes. Being a connecting link between molecular chaperones and 26S proteasomes, it is widely regarded as the central player in the cellular protein quality control system. Recent analyses have provided new insights on the biochemical and functional dynamics of CHIP. In this review article, we give a comprehensive account of our current knowledge on the biology of CHIP, which apart from shedding light on fundamental biological questions promises to provide a potential target for therapeutic intervention.

Keywords: Cancer; Neurological disorder; Physiology; STUB1.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Aging / physiology
DNA Damage / physiology
Humans
Molecular Chaperones / metabolism*
Neoplasms / metabolism
Oxidative Stress / physiology
Ubiquitin-Protein Ligases / metabolism*

Substances

Molecular Chaperones
STUB1 protein, human
Ubiquitin-Protein Ligases