The Chemical Biology of Reversible Lysine Post-translational Modifications
Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the “writers,” “erasers,” and “readers”...
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| Veröffentlicht in: | Cell chemical biology 2020-08, Vol.27 (8), p.953-969 |
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| container_title | Cell chemical biology |
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| creator | Wang, Zhipeng A. Cole, Philip A. |
| description | Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the “writers,” “erasers,” and “readers” of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologies, that have helped to delineate Lys PTM functions and show promise for a diverse set of biomedical applications.
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Zhipeng Wang and Philip Cole review major types of chemical modifications of the amino acid lysine in proteins and how they are added and removed. They also discuss a number of chemical approaches and how they have been applied to clarify the roles of lysine modifications in biology and medicine. |
| doi_str_mv | 10.1016/j.chembiol.2020.07.002 |
| format | Article |
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Zhipeng Wang and Philip Cole review major types of chemical modifications of the amino acid lysine in proteins and how they are added and removed. They also discuss a number of chemical approaches and how they have been applied to clarify the roles of lysine modifications in biology and medicine.</description><identifier>ISSN: 2451-9456</identifier><identifier>EISSN: 2451-9448</identifier><identifier>EISSN: 2451-9456</identifier><identifier>DOI: 10.1016/j.chembiol.2020.07.002</identifier><identifier>PMID: 32698016</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>acetylation ; acetyltransferase ; bromodomain ; deacetylase ; enzyme ; methylation ; ubiquitination</subject><ispartof>Cell chemical biology, 2020-08, Vol.27 (8), p.953-969</ispartof><rights>2020 Elsevier Ltd</rights><rights>Copyright © 2020 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c537t-fa4044d7c392846c48060bb2dfe3ca30e4755d60247a7fdad4dc01ba5f17f5bb3</citedby><cites>FETCH-LOGICAL-c537t-fa4044d7c392846c48060bb2dfe3ca30e4755d60247a7fdad4dc01ba5f17f5bb3</cites><orcidid>0000-0002-5693-7359</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32698016$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Zhipeng A.</creatorcontrib><creatorcontrib>Cole, Philip A.</creatorcontrib><title>The Chemical Biology of Reversible Lysine Post-translational Modifications</title><title>Cell chemical biology</title><addtitle>Cell Chem Biol</addtitle><description>Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the “writers,” “erasers,” and “readers” of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologies, that have helped to delineate Lys PTM functions and show promise for a diverse set of biomedical applications.
[Display omitted]
Zhipeng Wang and Philip Cole review major types of chemical modifications of the amino acid lysine in proteins and how they are added and removed. They also discuss a number of chemical approaches and how they have been applied to clarify the roles of lysine modifications in biology and medicine.</description><subject>acetylation</subject><subject>acetyltransferase</subject><subject>bromodomain</subject><subject>deacetylase</subject><subject>enzyme</subject><subject>methylation</subject><subject>ubiquitination</subject><issn>2451-9456</issn><issn>2451-9448</issn><issn>2451-9456</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNqFkE1OwzAQhS0Eoqj0ClUukDBOnDjZIKDiV0UgVNaWY49bV2lcxaFSb4-r0gpWrGZGfu8bzyNkTCGhQIurZaIWuKqta5IUUkiAJwDpCblIWU7jirHy9NjnxYCMvF8CBGfGacbPySBLi6oM8wV5mS0wmgSaVbKJ7gLSzbeRM9EHbrDztm4wmm69bTF6d76P-062vpG9dW3QvzptTXDuRn9JzoxsPI5-6pB8PtzPJk_x9O3xeXI7jVWe8T42kgFjmqusSktWKFZCAXWdaoOZkhkg43muC0gZl9xoqZlWQGuZG8pNXtfZkFzvueuveoVaYRs-1Yh1Z1ey2wonrfj70tqFmLuN4KwM91cBUOwBqnPed2iOXgpiF7BYikPAYhewAC5CwME4_r35aDvEGQQ3ewGG-zcWO-GVxVahth2qXmhn_9vxDZn3khE</recordid><startdate>20200820</startdate><enddate>20200820</enddate><creator>Wang, Zhipeng A.</creator><creator>Cole, Philip A.</creator><general>Elsevier Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5693-7359</orcidid></search><sort><creationdate>20200820</creationdate><title>The Chemical Biology of Reversible Lysine Post-translational Modifications</title><author>Wang, Zhipeng A. ; Cole, Philip A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c537t-fa4044d7c392846c48060bb2dfe3ca30e4755d60247a7fdad4dc01ba5f17f5bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>acetylation</topic><topic>acetyltransferase</topic><topic>bromodomain</topic><topic>deacetylase</topic><topic>enzyme</topic><topic>methylation</topic><topic>ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Zhipeng A.</creatorcontrib><creatorcontrib>Cole, Philip A.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Zhipeng A.</au><au>Cole, Philip A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Chemical Biology of Reversible Lysine Post-translational Modifications</atitle><jtitle>Cell chemical biology</jtitle><addtitle>Cell Chem Biol</addtitle><date>2020-08-20</date><risdate>2020</risdate><volume>27</volume><issue>8</issue><spage>953</spage><epage>969</epage><pages>953-969</pages><issn>2451-9456</issn><eissn>2451-9448</eissn><eissn>2451-9456</eissn><abstract>Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the “writers,” “erasers,” and “readers” of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologies, that have helped to delineate Lys PTM functions and show promise for a diverse set of biomedical applications.
[Display omitted]
Zhipeng Wang and Philip Cole review major types of chemical modifications of the amino acid lysine in proteins and how they are added and removed. They also discuss a number of chemical approaches and how they have been applied to clarify the roles of lysine modifications in biology and medicine.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>32698016</pmid><doi>10.1016/j.chembiol.2020.07.002</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0002-5693-7359</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | acetylation acetyltransferase bromodomain deacetylase enzyme methylation ubiquitination |
| title | The Chemical Biology of Reversible Lysine Post-translational Modifications |
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