Widespread arginine phosphorylation in human cells—a novel protein PTM revealed by mass spectrometry
Arginine phosphorylation (pArg) is recently discovered as a ubiquitous protein N -phosphorylation in bacteria. However, its prevalence and roles in mammalian cells remain largely unknown due to the lack of established workflow and the inherent lability of phosphoramidate (P–N) bond. Emerging evidenc...
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| Veröffentlicht in: | Science China. Chemistry 2020-03, Vol.63 (3), p.341-346 |
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| creator | Fu, Songsen Fu, Chuan Zhou, Quan Lin, Rongcan Ouyang, Han Wang, Minning Sun, Ying Liu, Yan Zhao, Yufen |
| description | Arginine phosphorylation (pArg) is recently discovered as a ubiquitous protein
N
-phosphorylation in bacteria. However, its prevalence and roles in mammalian cells remain largely unknown due to the lack of established workflow and the inherent lability of phosphoramidate (P–N) bond. Emerging evidences suggest that
N
-phosphorylation may extensively exist in eu-karyotes and play crucial roles. We report a phosphoproteomic workflow, which allows for the first time revealing the widespread occurrence of pArg in human cells by mass spectrometry. By virtue of this approach, we identified 152 high-confidence pArg sites derived from 118 proteins. Remarkably, the discovered pArg phosphorylation motif and gene ontology hint a possible cellular function of arginine phosphorylation which may regulate the favorability of propeptide convertase substrate. The obtained pArg dataset paves a way for a better understanding of the biological functions of eukaryotic pArg in the future. |
| doi_str_mv | 10.1007/s11426-019-9656-7 |
| format | Article |
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N
-phosphorylation in bacteria. However, its prevalence and roles in mammalian cells remain largely unknown due to the lack of established workflow and the inherent lability of phosphoramidate (P–N) bond. Emerging evidences suggest that
N
-phosphorylation may extensively exist in eu-karyotes and play crucial roles. We report a phosphoproteomic workflow, which allows for the first time revealing the widespread occurrence of pArg in human cells by mass spectrometry. By virtue of this approach, we identified 152 high-confidence pArg sites derived from 118 proteins. Remarkably, the discovered pArg phosphorylation motif and gene ontology hint a possible cellular function of arginine phosphorylation which may regulate the favorability of propeptide convertase substrate. The obtained pArg dataset paves a way for a better understanding of the biological functions of eukaryotic pArg in the future.</description><identifier>ISSN: 1674-7291</identifier><identifier>EISSN: 1869-1870</identifier><identifier>DOI: 10.1007/s11426-019-9656-7</identifier><language>eng</language><publisher>Beijing: Science China Press</publisher><subject>Acids ; Biology ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Gram-positive bacteria ; Kinases ; Mass spectrometry ; Peptides ; Phosphatase ; Phosphorylation ; Proteins ; Proteomics ; Scientific imaging ; Substrates ; Workflow</subject><ispartof>Science China. Chemistry, 2020-03, Vol.63 (3), p.341-346</ispartof><rights>Science China Press and Springer-Verlag GmbH Germany, part of Springer Nature 2020</rights><rights>Science China Press and Springer-Verlag GmbH Germany, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c359t-f4340551e510d9f9d94a416d1b09d7708e3fc095038a8531c8fec7f0c0b2bd673</citedby><cites>FETCH-LOGICAL-c359t-f4340551e510d9f9d94a416d1b09d7708e3fc095038a8531c8fec7f0c0b2bd673</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11426-019-9656-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2918581753?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,776,780,21367,27901,27902,33721,41464,42533,43781,51294</link.rule.ids></links><search><creatorcontrib>Fu, Songsen</creatorcontrib><creatorcontrib>Fu, Chuan</creatorcontrib><creatorcontrib>Zhou, Quan</creatorcontrib><creatorcontrib>Lin, Rongcan</creatorcontrib><creatorcontrib>Ouyang, Han</creatorcontrib><creatorcontrib>Wang, Minning</creatorcontrib><creatorcontrib>Sun, Ying</creatorcontrib><creatorcontrib>Liu, Yan</creatorcontrib><creatorcontrib>Zhao, Yufen</creatorcontrib><title>Widespread arginine phosphorylation in human cells—a novel protein PTM revealed by mass spectrometry</title><title>Science China. Chemistry</title><addtitle>Sci. China Chem</addtitle><description>Arginine phosphorylation (pArg) is recently discovered as a ubiquitous protein
N
-phosphorylation in bacteria. However, its prevalence and roles in mammalian cells remain largely unknown due to the lack of established workflow and the inherent lability of phosphoramidate (P–N) bond. Emerging evidences suggest that
N
-phosphorylation may extensively exist in eu-karyotes and play crucial roles. We report a phosphoproteomic workflow, which allows for the first time revealing the widespread occurrence of pArg in human cells by mass spectrometry. By virtue of this approach, we identified 152 high-confidence pArg sites derived from 118 proteins. Remarkably, the discovered pArg phosphorylation motif and gene ontology hint a possible cellular function of arginine phosphorylation which may regulate the favorability of propeptide convertase substrate. The obtained pArg dataset paves a way for a better understanding of the biological functions of eukaryotic pArg in the future.</description><subject>Acids</subject><subject>Biology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Gram-positive bacteria</subject><subject>Kinases</subject><subject>Mass spectrometry</subject><subject>Peptides</subject><subject>Phosphatase</subject><subject>Phosphorylation</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Scientific imaging</subject><subject>Substrates</subject><subject>Workflow</subject><issn>1674-7291</issn><issn>1869-1870</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp1kM1qwzAMx83YYKXrA-xm2DmbHMexfRxlX9CxHTp2NE6itCn5mp0WcttD7An3JHPJYKcJhASS_pJ-hFwyuGYA8sYzlsRpBExHOhVpJE_IjKlUR0xJOA15KpNIxpqdk4X3OwjGOcRSzEj5XhXoe4e2oNZtqrZqkfbbzgd3Y22Hqmtp1dLtvrEtzbGu_ffnl6Vtd8Ca9q4bMFRf18_U4QFtjQXNRtpY76nvMR9c1-DgxgtyVtra4-I3zsnb_d16-RitXh6elrerKOdCD1GZ8ASEYCgYFLrUhU5swtKCZaALKUEhL3PQAriySnCWqxJzWUIOWZwVqeRzcjXphss-9ugHs-v2rg0rTXhfCcWk4KGLTV2567x3WJreVY11o2FgjkTNRNQEouZI1ByV42kmwKraDbo_5f-HfgCSKXqk</recordid><startdate>20200301</startdate><enddate>20200301</enddate><creator>Fu, Songsen</creator><creator>Fu, Chuan</creator><creator>Zhou, Quan</creator><creator>Lin, Rongcan</creator><creator>Ouyang, Han</creator><creator>Wang, Minning</creator><creator>Sun, Ying</creator><creator>Liu, Yan</creator><creator>Zhao, Yufen</creator><general>Science China Press</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7XB</scope><scope>88I</scope><scope>8FE</scope><scope>8FG</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>KB.</scope><scope>M2P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>20200301</creationdate><title>Widespread arginine phosphorylation in human cells—a novel protein PTM revealed by mass spectrometry</title><author>Fu, Songsen ; 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Chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fu, Songsen</au><au>Fu, Chuan</au><au>Zhou, Quan</au><au>Lin, Rongcan</au><au>Ouyang, Han</au><au>Wang, Minning</au><au>Sun, Ying</au><au>Liu, Yan</au><au>Zhao, Yufen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Widespread arginine phosphorylation in human cells—a novel protein PTM revealed by mass spectrometry</atitle><jtitle>Science China. Chemistry</jtitle><stitle>Sci. China Chem</stitle><date>2020-03-01</date><risdate>2020</risdate><volume>63</volume><issue>3</issue><spage>341</spage><epage>346</epage><pages>341-346</pages><issn>1674-7291</issn><eissn>1869-1870</eissn><abstract>Arginine phosphorylation (pArg) is recently discovered as a ubiquitous protein
N
-phosphorylation in bacteria. However, its prevalence and roles in mammalian cells remain largely unknown due to the lack of established workflow and the inherent lability of phosphoramidate (P–N) bond. Emerging evidences suggest that
N
-phosphorylation may extensively exist in eu-karyotes and play crucial roles. We report a phosphoproteomic workflow, which allows for the first time revealing the widespread occurrence of pArg in human cells by mass spectrometry. By virtue of this approach, we identified 152 high-confidence pArg sites derived from 118 proteins. Remarkably, the discovered pArg phosphorylation motif and gene ontology hint a possible cellular function of arginine phosphorylation which may regulate the favorability of propeptide convertase substrate. The obtained pArg dataset paves a way for a better understanding of the biological functions of eukaryotic pArg in the future.</abstract><cop>Beijing</cop><pub>Science China Press</pub><doi>10.1007/s11426-019-9656-7</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acids Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Gram-positive bacteria Kinases Mass spectrometry Peptides Phosphatase Phosphorylation Proteins Proteomics Scientific imaging Substrates Workflow |
| title | Widespread arginine phosphorylation in human cells—a novel protein PTM revealed by mass spectrometry |
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