Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3.
Homo sapiens J domain protein (HSJ1) is a J-domain containing co-chaperone that is known to stimulate ATPase activity of HSP70 chaperone, while it also harbors two ubiquitin (Ub)-interacting motifs (UIMs) that may bind with ubiquitinated substrates and potentially function in protein degradation. We...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3098244?pdf=render |
| _version_ | 1818978136026513408 |
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| author | Xue-Chao Gao Chen-Jie Zhou Zi-Ren Zhou Yu-Hang Zhang Xue-Ming Zheng Ai-Xin Song Hong-Yu Hu |
| author_facet | Xue-Chao Gao Chen-Jie Zhou Zi-Ren Zhou Yu-Hang Zhang Xue-Ming Zheng Ai-Xin Song Hong-Yu Hu |
| author_sort | Xue-Chao Gao |
| collection | DOAJ |
| description | Homo sapiens J domain protein (HSJ1) is a J-domain containing co-chaperone that is known to stimulate ATPase activity of HSP70 chaperone, while it also harbors two ubiquitin (Ub)-interacting motifs (UIMs) that may bind with ubiquitinated substrates and potentially function in protein degradation. We studied the effects of HSJ1a on the protein levels of both normal and the disease--related polyQ-expanded forms of ataxin-3 (Atx3) in cells. The results demonstrate that the N-terminal J-domain and the C-terminal UIM domain of HSJ1a exert opposite functions in regulating the protein level of cellular overexpressed Atx3. This dual regulation is dependent on the binding of the J-domain with HSP70, and the UIM domain with polyUb chains. The J-domain down-regulates the protein level of Atx3 through HSP70 mediated proteasomal degradation, while the UIM domain may alleviate this process via maintaining the ubiquitinated Atx3. We propose that co-chaperone HSJ1a orchestrates the balance of substrates in stressed cells in a Yin-Yang manner. |
| first_indexed | 2024-12-20T16:38:50Z |
| format | Article |
| id | doaj.art-cf325139065c4d9896fad4999e4a6941 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T16:38:50Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-cf325139065c4d9896fad4999e4a69412022-12-21T19:33:06ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0165e1976310.1371/journal.pone.0019763Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3.Xue-Chao GaoChen-Jie ZhouZi-Ren ZhouYu-Hang ZhangXue-Ming ZhengAi-Xin SongHong-Yu HuHomo sapiens J domain protein (HSJ1) is a J-domain containing co-chaperone that is known to stimulate ATPase activity of HSP70 chaperone, while it also harbors two ubiquitin (Ub)-interacting motifs (UIMs) that may bind with ubiquitinated substrates and potentially function in protein degradation. We studied the effects of HSJ1a on the protein levels of both normal and the disease--related polyQ-expanded forms of ataxin-3 (Atx3) in cells. The results demonstrate that the N-terminal J-domain and the C-terminal UIM domain of HSJ1a exert opposite functions in regulating the protein level of cellular overexpressed Atx3. This dual regulation is dependent on the binding of the J-domain with HSP70, and the UIM domain with polyUb chains. The J-domain down-regulates the protein level of Atx3 through HSP70 mediated proteasomal degradation, while the UIM domain may alleviate this process via maintaining the ubiquitinated Atx3. We propose that co-chaperone HSJ1a orchestrates the balance of substrates in stressed cells in a Yin-Yang manner.http://europepmc.org/articles/PMC3098244?pdf=render |
| spellingShingle | Xue-Chao Gao Chen-Jie Zhou Zi-Ren Zhou Yu-Hang Zhang Xue-Ming Zheng Ai-Xin Song Hong-Yu Hu Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3. PLoS ONE |
| title | Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3. |
| title_full | Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3. |
| title_fullStr | Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3. |
| title_full_unstemmed | Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3. |
| title_short | Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3. |
| title_sort | co chaperone hsj1a dually regulates the proteasomal degradation of ataxin 3 |
| url | http://europepmc.org/articles/PMC3098244?pdf=render |
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