Cargando…
The E3 Ligase CHIP: Insights into Its Structure and Regulation
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 regulate...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017836/ https://www.ncbi.nlm.nih.gov/pubmed/24868554 http://dx.doi.org/10.1155/2014/918183 |
_version_ | 1782480015153168384 |
---|---|
author | Paul, Indranil Ghosh, Mrinal K. |
author_facet | Paul, Indranil Ghosh, Mrinal K. |
author_sort | Paul, Indranil |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4017836 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-40178362014-05-27 The E3 Ligase CHIP: Insights into Its Structure and Regulation Paul, Indranil Ghosh, Mrinal K. Biomed Res Int Review Article 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. Hindawi Publishing Corporation 2014 2014-04-24 /pmc/articles/PMC4017836/ /pubmed/24868554 http://dx.doi.org/10.1155/2014/918183 Text en Copyright © 2014 I. Paul and M. K. Ghosh. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Paul, Indranil Ghosh, Mrinal K. The E3 Ligase CHIP: Insights into Its Structure and Regulation |
title | The E3 Ligase CHIP: Insights into Its Structure and Regulation |
title_full | The E3 Ligase CHIP: Insights into Its Structure and Regulation |
title_fullStr | The E3 Ligase CHIP: Insights into Its Structure and Regulation |
title_full_unstemmed | The E3 Ligase CHIP: Insights into Its Structure and Regulation |
title_short | The E3 Ligase CHIP: Insights into Its Structure and Regulation |
title_sort | e3 ligase chip: insights into its structure and regulation |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017836/ https://www.ncbi.nlm.nih.gov/pubmed/24868554 http://dx.doi.org/10.1155/2014/918183 |
work_keys_str_mv | AT paulindranil thee3ligasechipinsightsintoitsstructureandregulation AT ghoshmrinalk thee3ligasechipinsightsintoitsstructureandregulation AT paulindranil e3ligasechipinsightsintoitsstructureandregulation AT ghoshmrinalk e3ligasechipinsightsintoitsstructureandregulation |