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BAG2 structure, function and involvement in disease

Bcl2-associated athanogene 2 (BAG2) shares a similar molecular structure and function with other BAG family members. Functioning as a co-chaperone, it interacts with the ATPase domain of the heat shock protein 70 (dHsp70) through its BAG domain. It also interacts with many other molecules and regula...

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Detalles Bibliográficos
Autores principales: Qin, Lixia, Guo, Jifeng, Zheng, Qian, Zhang, Hainan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5415834/
https://www.ncbi.nlm.nih.gov/pubmed/28536620
http://dx.doi.org/10.1186/s11658-016-0020-2
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author Qin, Lixia
Guo, Jifeng
Zheng, Qian
Zhang, Hainan
author_facet Qin, Lixia
Guo, Jifeng
Zheng, Qian
Zhang, Hainan
author_sort Qin, Lixia
collection PubMed
description Bcl2-associated athanogene 2 (BAG2) shares a similar molecular structure and function with other BAG family members. Functioning as a co-chaperone, it interacts with the ATPase domain of the heat shock protein 70 (dHsp70) through its BAG domain. It also interacts with many other molecules and regulates various cellular functions. An increasing number of studies have indicated that BAG2 is involved in the pathogenesis of various diseases, including cancers and neurodegenerative diseases. This paper is a comprehensive review of the structure, functions, and protein interactions of BAG2. We also discuss its roles in diseases, including cancer, Alzheimer’s disease, Parkinson’s disease and spinocerebellar ataxia type-3. Further research on BAG2 could lead to an understanding of the pathogenesis of these disorders or even to novel therapeutic approaches.
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spelling pubmed-54158342017-05-23 BAG2 structure, function and involvement in disease Qin, Lixia Guo, Jifeng Zheng, Qian Zhang, Hainan Cell Mol Biol Lett Mini Review Bcl2-associated athanogene 2 (BAG2) shares a similar molecular structure and function with other BAG family members. Functioning as a co-chaperone, it interacts with the ATPase domain of the heat shock protein 70 (dHsp70) through its BAG domain. It also interacts with many other molecules and regulates various cellular functions. An increasing number of studies have indicated that BAG2 is involved in the pathogenesis of various diseases, including cancers and neurodegenerative diseases. This paper is a comprehensive review of the structure, functions, and protein interactions of BAG2. We also discuss its roles in diseases, including cancer, Alzheimer’s disease, Parkinson’s disease and spinocerebellar ataxia type-3. Further research on BAG2 could lead to an understanding of the pathogenesis of these disorders or even to novel therapeutic approaches. BioMed Central 2016-09-20 /pmc/articles/PMC5415834/ /pubmed/28536620 http://dx.doi.org/10.1186/s11658-016-0020-2 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Mini Review
Qin, Lixia
Guo, Jifeng
Zheng, Qian
Zhang, Hainan
BAG2 structure, function and involvement in disease
title BAG2 structure, function and involvement in disease
title_full BAG2 structure, function and involvement in disease
title_fullStr BAG2 structure, function and involvement in disease
title_full_unstemmed BAG2 structure, function and involvement in disease
title_short BAG2 structure, function and involvement in disease
title_sort bag2 structure, function and involvement in disease
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5415834/
https://www.ncbi.nlm.nih.gov/pubmed/28536620
http://dx.doi.org/10.1186/s11658-016-0020-2
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