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Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones
The discovery of heat shock proteins shaped our view of protein folding in the cell. Since their initial discovery, chaperone proteins were identified in all domains of life, demonstrating their vital and conserved functional roles in protein homeostasis. Chaperone proteins maintain proper protein f...
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| Published in: | International journal of molecular sciences 2019-08, Vol.20 (17), p.4207 |
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| container_title | International journal of molecular sciences |
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| creator | Griffith, Alijah A Holmes, William |
| description | The discovery of heat shock proteins shaped our view of protein folding in the cell. Since their initial discovery, chaperone proteins were identified in all domains of life, demonstrating their vital and conserved functional roles in protein homeostasis. Chaperone proteins maintain proper protein folding in the cell by utilizing a variety of distinct, characteristic mechanisms to prevent aberrant intermolecular interactions, prevent protein aggregation, and lower entropic costs to allow for protein refolding. Continued study has found that chaperones may exhibit alternative functions, including maintaining protein folding during endoplasmic reticulum (ER) import and chaperone-mediated degradation, among others. Alternative chaperone functions are frequently controlled by post-translational modification, in which a given chaperone can switch between functions through covalent modification. This review will focus on the Hsp70 class chaperones and their Hsp40 co-chaperones, specifically highlighting the importance of post-translational control of chaperones. These modifications may serve as a target for therapeutic intervention in the treatment of diseases of protein misfolding and aggregation. |
| doi_str_mv | 10.3390/ijms20174207 |
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Since their initial discovery, chaperone proteins were identified in all domains of life, demonstrating their vital and conserved functional roles in protein homeostasis. Chaperone proteins maintain proper protein folding in the cell by utilizing a variety of distinct, characteristic mechanisms to prevent aberrant intermolecular interactions, prevent protein aggregation, and lower entropic costs to allow for protein refolding. Continued study has found that chaperones may exhibit alternative functions, including maintaining protein folding during endoplasmic reticulum (ER) import and chaperone-mediated degradation, among others. Alternative chaperone functions are frequently controlled by post-translational modification, in which a given chaperone can switch between functions through covalent modification. This review will focus on the Hsp70 class chaperones and their Hsp40 co-chaperones, specifically highlighting the importance of post-translational control of chaperones. 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Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 by the authors. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c478t-1fd27905cef585c7e34e439cb873200a58a2576e697455d11d699e625d8aa4223</citedby><cites>FETCH-LOGICAL-c478t-1fd27905cef585c7e34e439cb873200a58a2576e697455d11d699e625d8aa4223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2332368219/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2332368219?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,74998</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31466231$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Griffith, Alijah A</creatorcontrib><creatorcontrib>Holmes, William</creatorcontrib><title>Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>The discovery of heat shock proteins shaped our view of protein folding in the cell. Since their initial discovery, chaperone proteins were identified in all domains of life, demonstrating their vital and conserved functional roles in protein homeostasis. Chaperone proteins maintain proper protein folding in the cell by utilizing a variety of distinct, characteristic mechanisms to prevent aberrant intermolecular interactions, prevent protein aggregation, and lower entropic costs to allow for protein refolding. Continued study has found that chaperones may exhibit alternative functions, including maintaining protein folding during endoplasmic reticulum (ER) import and chaperone-mediated degradation, among others. Alternative chaperone functions are frequently controlled by post-translational modification, in which a given chaperone can switch between functions through covalent modification. This review will focus on the Hsp70 class chaperones and their Hsp40 co-chaperones, specifically highlighting the importance of post-translational control of chaperones. These modifications may serve as a target for therapeutic intervention in the treatment of diseases of protein misfolding and aggregation.</description><subject>Adenosine triphosphatase</subject><subject>Allosteric Regulation</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Binding</subject><subject>Binding sites</subject><subject>chaperone proteins</subject><subject>Chaperones</subject><subject>Cytoplasm</subject><subject>Domains</subject><subject>Endoplasmic reticulum</subject><subject>Enzymes</subject><subject>Gene expression</subject><subject>Hsp70</subject><subject>HSP70 Heat-Shock Proteins - chemistry</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Hsp70 protein</subject><subject>Humans</subject><subject>Hydrophobicity</subject><subject>Localization</subject><subject>Lysine</subject><subject>Nucleotides</subject><subject>Phosphorylation</subject><subject>Polarity</subject><subject>Post-translation</subject><subject>post-translational modifications</subject><subject>Protein folding</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Residues</subject><subject>Review</subject><subject>Structure-function relationships</subject><subject>Translation</subject><subject>Ubiquitin</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdkc9rFDEUx4MotlZvnmXAiwdH8_tNPAiytLZY0cN6DpnMyzbL7GRNZgT_e2O3lq0QyK8PH957X0JeMvpOCEPfx-2ucMpAcgqPyCmTnLeUanh8dD4hz0rZUsoFV-YpORFMas0FOyVfLuKEzXqZ4rT50JyHgH4uTQrN91Tmdp3dVEY3xzS5sfmahhiiv702dV2WPdBmdeP2mNOE5Tl5EtxY8MXdfkZ-XJyvV5ft9bfPV6tP162X0M0tCwMHQ5XHoDrlAYVEKYzvOxCcUqc6xxVo1AakUgNjgzYGNVdD51ztSJyRq4N3SG5r9znuXP5tk4v29iHljXV5jn5E2wN0PQ8gAJiEoe-BUxOc8cxhr1Woro8H137pdzh4nObsxgfShz9TvLGb9MtqkHXkugre3Aly-rlgme0uFo_j6CZMS7Gcd4IxpQSt6Ov_0G1acp1spYTgQnecmUq9PVA-p1IyhvtiGLV_E7fHiVf81XED9_C_iMUf_FmlSQ</recordid><startdate>20190828</startdate><enddate>20190828</enddate><creator>Griffith, Alijah A</creator><creator>Holmes, William</creator><general>MDPI AG</general><general>MDPI</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20190828</creationdate><title>Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones</title><author>Griffith, Alijah A ; Holmes, William</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-1fd27905cef585c7e34e439cb873200a58a2576e697455d11d699e625d8aa4223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Adenosine triphosphatase</topic><topic>Allosteric Regulation</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Binding</topic><topic>Binding sites</topic><topic>chaperone proteins</topic><topic>Chaperones</topic><topic>Cytoplasm</topic><topic>Domains</topic><topic>Endoplasmic reticulum</topic><topic>Enzymes</topic><topic>Gene expression</topic><topic>Hsp70</topic><topic>HSP70 Heat-Shock Proteins - chemistry</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Hsp70 protein</topic><topic>Humans</topic><topic>Hydrophobicity</topic><topic>Localization</topic><topic>Lysine</topic><topic>Nucleotides</topic><topic>Phosphorylation</topic><topic>Polarity</topic><topic>Post-translation</topic><topic>post-translational modifications</topic><topic>Protein folding</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Residues</topic><topic>Review</topic><topic>Structure-function relationships</topic><topic>Translation</topic><topic>Ubiquitin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Griffith, Alijah A</creatorcontrib><creatorcontrib>Holmes, William</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest_Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Open Access: DOAJ - Directory of Open Access Journals</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Griffith, Alijah A</au><au>Holmes, William</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2019-08-28</date><risdate>2019</risdate><volume>20</volume><issue>17</issue><spage>4207</spage><pages>4207-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>The discovery of heat shock proteins shaped our view of protein folding in the cell. 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| subjects | Adenosine triphosphatase Allosteric Regulation Amino acids Animals Binding Binding sites chaperone proteins Chaperones Cytoplasm Domains Endoplasmic reticulum Enzymes Gene expression Hsp70 HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - metabolism Hsp70 protein Humans Hydrophobicity Localization Lysine Nucleotides Phosphorylation Polarity Post-translation post-translational modifications Protein folding Protein Processing, Post-Translational Proteins Residues Review Structure-function relationships Translation Ubiquitin |
| title | Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones |
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