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...
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| Veröffentlicht in: | PloS one 2011-05, Vol.6 (5), p.e19763-e19763 |
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| creator | Gao, Xue-Chao Zhou, Chen-Jie Zhou, Zi-Ren Zhang, Yu-Hang Zheng, Xue-Ming Song, Ai-Xin Hu, Hong-Yu |
| 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. |
| doi_str_mv | 10.1371/journal.pone.0019763 |
| format | Article |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0019763</identifier><identifier>PMID: 21625540</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adenosine triphosphatase ; Alzheimer's disease ; Apoptosis ; Ataxia ; Ataxin ; Ataxin-3 ; Biochemistry ; Biodegradation ; Biology ; Blotting, Western ; Cells, Cultured ; Degradation ; E coli ; Escherichia coli ; Heat shock proteins ; Homeostasis ; HSP40 Heat-Shock Proteins - metabolism ; HSP70 Heat-Shock Proteins - metabolism ; Hsp70 protein ; Humans ; Immunoenzyme Techniques ; Immunoprecipitation ; Kidney - cytology ; Kidney - metabolism ; Kinases ; Laboratories ; Molecular biology ; Molecular Chaperones - metabolism ; Nerve Tissue Proteins - metabolism ; Nuclear Proteins - metabolism ; Polyglutamine diseases ; Proteasome Endopeptidase Complex - metabolism ; Proteasomes ; Protein Binding ; Protein folding ; Protein Structure, Tertiary ; Proteolysis ; Repressor Proteins - metabolism ; Stress response ; Substrates ; Trinucleotide repeat diseases ; Ubiquitin ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases - metabolism</subject><ispartof>PloS one, 2011-05, Vol.6 (5), p.e19763-e19763</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Gao et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Gao et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c691t-a57224ccb7a35b5a1d877c61530dd96af0685e49adc2bf50c6c91005734ea0e43</citedby><cites>FETCH-LOGICAL-c691t-a57224ccb7a35b5a1d877c61530dd96af0685e49adc2bf50c6c91005734ea0e43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3098244/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3098244/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2095,2914,23846,27903,27904,53770,53772,79347,79348</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21625540$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Chu, Charleen T.</contributor><creatorcontrib>Gao, Xue-Chao</creatorcontrib><creatorcontrib>Zhou, Chen-Jie</creatorcontrib><creatorcontrib>Zhou, Zi-Ren</creatorcontrib><creatorcontrib>Zhang, Yu-Hang</creatorcontrib><creatorcontrib>Zheng, Xue-Ming</creatorcontrib><creatorcontrib>Song, Ai-Xin</creatorcontrib><creatorcontrib>Hu, Hong-Yu</creatorcontrib><title>Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3</title><title>PloS one</title><addtitle>PLoS One</addtitle><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. 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We propose that co-chaperone HSJ1a orchestrates the balance of substrates in stressed cells in a Yin-Yang manner.</description><subject>Adenosine triphosphatase</subject><subject>Alzheimer's disease</subject><subject>Apoptosis</subject><subject>Ataxia</subject><subject>Ataxin</subject><subject>Ataxin-3</subject><subject>Biochemistry</subject><subject>Biodegradation</subject><subject>Biology</subject><subject>Blotting, Western</subject><subject>Cells, Cultured</subject><subject>Degradation</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Heat shock proteins</subject><subject>Homeostasis</subject><subject>HSP40 Heat-Shock Proteins - metabolism</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Hsp70 protein</subject><subject>Humans</subject><subject>Immunoenzyme Techniques</subject><subject>Immunoprecipitation</subject><subject>Kidney - cytology</subject><subject>Kidney - metabolism</subject><subject>Kinases</subject><subject>Laboratories</subject><subject>Molecular biology</subject><subject>Molecular Chaperones - metabolism</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nuclear Proteins - metabolism</subject><subject>Polyglutamine diseases</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Proteasomes</subject><subject>Protein Binding</subject><subject>Protein folding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteolysis</subject><subject>Repressor Proteins - metabolism</subject><subject>Stress response</subject><subject>Substrates</subject><subject>Trinucleotide repeat diseases</subject><subject>Ubiquitin</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNku9r1DAYx4sobk7_A9GCoPiiZ9L8aPNGGIe608HAqW_Dc0na68g1tySV7b839bpxlb2QFFKSz_ebJ0--WfYSowUmFf5w5Qbfg13sXG8WCGFRcfIoO8aClAUvEXl88H-UPQvhCiFGas6fZkcl5iVjFB1n35auUBvYGZ9s8rPLrxhyPYC1t7k37WAhmpDHjcl33kUDwW3B5tq0HjTEzvW5a3KIcNP1BXmePWnABvNimk-yn58__VieFecXX1bL0_NCcYFjAawqS6rUugLC1gywrqtKccwI0lpwaBCvmaECtCrXDUOKK4FT7RWhBpCh5CR7vffdWRfk1IcgcSlqQpBgOBGrPaEdXMmd77bgb6WDTv5dcL6V4GOnrJGqIWVSCMSZolrUgjegqRDCUOCCjl4fp9OG9dZoZfrowc5M5zt9t5Gt-y1TKXVJx3LfTQbeXQ8mRLntgjLWQm_cEGTNBavr9CXyzT_kw5ebqBZS_V3fuHSsGj3lKa14LTDmPFGLB6g0tNl2Kj1206X1meD9TJCYaG5iC0MIcnX5_f_Zi19z9u0BuzFg4yY4O4zpCXOQ7kHlXQjeNPc9xkiOkb_rhhwjL6fIJ9mrw_e5F91lnPwBSAj57A</recordid><startdate>20110519</startdate><enddate>20110519</enddate><creator>Gao, Xue-Chao</creator><creator>Zhou, Chen-Jie</creator><creator>Zhou, Zi-Ren</creator><creator>Zhang, Yu-Hang</creator><creator>Zheng, Xue-Ming</creator><creator>Song, Ai-Xin</creator><creator>Hu, Hong-Yu</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110519</creationdate><title>Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3</title><author>Gao, Xue-Chao ; Zhou, Chen-Jie ; Zhou, Zi-Ren ; Zhang, Yu-Hang ; Zheng, Xue-Ming ; Song, Ai-Xin ; Hu, Hong-Yu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c691t-a57224ccb7a35b5a1d877c61530dd96af0685e49adc2bf50c6c91005734ea0e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adenosine triphosphatase</topic><topic>Alzheimer's disease</topic><topic>Apoptosis</topic><topic>Ataxia</topic><topic>Ataxin</topic><topic>Ataxin-3</topic><topic>Biochemistry</topic><topic>Biodegradation</topic><topic>Biology</topic><topic>Blotting, Western</topic><topic>Cells, Cultured</topic><topic>Degradation</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Heat shock proteins</topic><topic>Homeostasis</topic><topic>HSP40 Heat-Shock Proteins - metabolism</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Hsp70 protein</topic><topic>Humans</topic><topic>Immunoenzyme Techniques</topic><topic>Immunoprecipitation</topic><topic>Kidney - cytology</topic><topic>Kidney - metabolism</topic><topic>Kinases</topic><topic>Laboratories</topic><topic>Molecular biology</topic><topic>Molecular Chaperones - metabolism</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nuclear Proteins - metabolism</topic><topic>Polyglutamine diseases</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Proteasomes</topic><topic>Protein Binding</topic><topic>Protein folding</topic><topic>Protein Structure, Tertiary</topic><topic>Proteolysis</topic><topic>Repressor Proteins - metabolism</topic><topic>Stress response</topic><topic>Substrates</topic><topic>Trinucleotide repeat diseases</topic><topic>Ubiquitin</topic><topic>Ubiquitin - metabolism</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gao, Xue-Chao</creatorcontrib><creatorcontrib>Zhou, Chen-Jie</creatorcontrib><creatorcontrib>Zhou, Zi-Ren</creatorcontrib><creatorcontrib>Zhang, Yu-Hang</creatorcontrib><creatorcontrib>Zheng, Xue-Ming</creatorcontrib><creatorcontrib>Song, Ai-Xin</creatorcontrib><creatorcontrib>Hu, Hong-Yu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gao, Xue-Chao</au><au>Zhou, Chen-Jie</au><au>Zhou, Zi-Ren</au><au>Zhang, Yu-Hang</au><au>Zheng, Xue-Ming</au><au>Song, Ai-Xin</au><au>Hu, Hong-Yu</au><au>Chu, Charleen T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-05-19</date><risdate>2011</risdate><volume>6</volume><issue>5</issue><spage>e19763</spage><epage>e19763</epage><pages>e19763-e19763</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21625540</pmid><doi>10.1371/journal.pone.0019763</doi><tpages>e19763</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine triphosphatase Alzheimer's disease Apoptosis Ataxia Ataxin Ataxin-3 Biochemistry Biodegradation Biology Blotting, Western Cells, Cultured Degradation E coli Escherichia coli Heat shock proteins Homeostasis HSP40 Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins - metabolism Hsp70 protein Humans Immunoenzyme Techniques Immunoprecipitation Kidney - cytology Kidney - metabolism Kinases Laboratories Molecular biology Molecular Chaperones - metabolism Nerve Tissue Proteins - metabolism Nuclear Proteins - metabolism Polyglutamine diseases Proteasome Endopeptidase Complex - metabolism Proteasomes Protein Binding Protein folding Protein Structure, Tertiary Proteolysis Repressor Proteins - metabolism Stress response Substrates Trinucleotide repeat diseases Ubiquitin Ubiquitin - metabolism Ubiquitin-Protein Ligases - metabolism |
| title | Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3 |
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