NFATc1 phosphorylation by DYRK1A increases its protein stability
NFATs are transcription factors involved in immune activation and tumor progression. Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional ac...
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| Veröffentlicht in: | PloS one 2017-02, Vol.12 (2), p.e0172985-e0172985 |
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| creator | Liu, Heng Wang, Ketao Chen, Shuai Sun, Qian Zhang, Yuankai Chen, Long Sun, Xiulian |
| description | NFATs are transcription factors involved in immune activation and tumor progression. Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional activity. DYRK1A phosphorylation of NFATc1/αA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation. Our results imply that DYRK1A is a positive kinase in regulation of NFATc1. |
| doi_str_mv | 10.1371/journal.pone.0172985 |
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Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional activity. DYRK1A phosphorylation of NFATc1/αA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation. Our results imply that DYRK1A is a positive kinase in regulation of NFATc1.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0172985</identifier><identifier>PMID: 28235034</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Motifs ; Analysis ; Biology and Life Sciences ; Cancer ; Cytoplasm ; Down syndrome ; Drosophila ; Dyrk Kinases ; Genetic aspects ; HEK293 Cells ; Humans ; Immune response ; Immunology ; Insects ; Kinases ; Lymphocytes ; Medicine and Health Sciences ; Monoclonal antibodies ; NFATC Transcription Factors - metabolism ; Otolaryngology ; Phosphorylation ; Physical Sciences ; Physiological aspects ; Proteasome Endopeptidase Complex - metabolism ; Proteasomes ; Protein expression ; Protein Serine-Threonine Kinases - metabolism ; Protein Stability ; Protein-Tyrosine Kinases - metabolism ; Proteins ; Proteolysis ; Research and Analysis Methods ; T cells ; Transcription factors ; Ubiquitin ; Ubiquitination</subject><ispartof>PloS one, 2017-02, Vol.12 (2), p.e0172985-e0172985</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 Liu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://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>2017 Liu et al 2017 Liu et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c791t-91200f340c7c45876977b89f46f19948b75c5c078bf77401c31efcc29efab4673</citedby><cites>FETCH-LOGICAL-c791t-91200f340c7c45876977b89f46f19948b75c5c078bf77401c31efcc29efab4673</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/PMC5325557/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5325557/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28235034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Reddy, Sakamuri V.</contributor><creatorcontrib>Liu, Heng</creatorcontrib><creatorcontrib>Wang, Ketao</creatorcontrib><creatorcontrib>Chen, Shuai</creatorcontrib><creatorcontrib>Sun, Qian</creatorcontrib><creatorcontrib>Zhang, Yuankai</creatorcontrib><creatorcontrib>Chen, Long</creatorcontrib><creatorcontrib>Sun, Xiulian</creatorcontrib><title>NFATc1 phosphorylation by DYRK1A increases its protein stability</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>NFATs are transcription factors involved in immune activation and tumor progression. Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional activity. DYRK1A phosphorylation of NFATc1/αA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation. Our results imply that DYRK1A is a positive kinase in regulation of NFATc1.</description><subject>Amino Acid Motifs</subject><subject>Analysis</subject><subject>Biology and Life Sciences</subject><subject>Cancer</subject><subject>Cytoplasm</subject><subject>Down syndrome</subject><subject>Drosophila</subject><subject>Dyrk Kinases</subject><subject>Genetic aspects</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Immune response</subject><subject>Immunology</subject><subject>Insects</subject><subject>Kinases</subject><subject>Lymphocytes</subject><subject>Medicine and Health Sciences</subject><subject>Monoclonal antibodies</subject><subject>NFATC Transcription Factors - metabolism</subject><subject>Otolaryngology</subject><subject>Phosphorylation</subject><subject>Physical Sciences</subject><subject>Physiological aspects</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Proteasomes</subject><subject>Protein expression</subject><subject>Protein Serine-Threonine Kinases - metabolism</subject><subject>Protein Stability</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Research and Analysis Methods</subject><subject>T cells</subject><subject>Transcription factors</subject><subject>Ubiquitin</subject><subject>Ubiquitination</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</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>eNqNk99rFDEQxxdRbK3-B6ILgujDnfm5SV7Eo1o9LBZqFXwK2Wz2LsfeZk2y4v33Znvbcit9KCEkTD7zzcwkk2XPIZhDzOC7jet9q5p551ozB5AhwemD7BgKjGYFAvjhwf4oexLCBgCKeVE8zo4QR5gCTI6zD9_OFlca5t3ahTT9rlHRujYvd_nHX5df4SK3rfZGBRNyG0PeeReNbfMQVWkbG3dPs0e1aoJ5Nq4n2Y-zT1enX2bnF5-Xp4vzmWYCxpmACIAaE6CZJpSzQjBWclGTooZCEF4yqqkGjJc1YwRAjaGptUbC1KokBcMn2cu9bte4IMfkg4ScQQ6AEDgRyz1RObWRnbdb5XfSKSuvDc6vpPLR6sZIIAihVVEzrDWBGAmCIVaqSlURAFckab0fb-vLram0aaNXzUR0etLatVy5P5JiRCkdwn0zCnj3uzchyq0N2jSNao3rr-NmHBLCxH1QRBlBxRDWq__QuwsxUiuVcrVt7VKIehCVC8IRJYBwmKj5HVQaldlanT5VbZN94vB24pCYaP7GlepDkMvvl_dnL35O2dcH7NqoJq6Da_rhH4YpSPag9i4Eb-rb94BADj1xUw059IQceyK5vTh8y1unmybA_wBVewLL</recordid><startdate>20170224</startdate><enddate>20170224</enddate><creator>Liu, Heng</creator><creator>Wang, Ketao</creator><creator>Chen, Shuai</creator><creator>Sun, Qian</creator><creator>Zhang, Yuankai</creator><creator>Chen, Long</creator><creator>Sun, Xiulian</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>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>20170224</creationdate><title>NFATc1 phosphorylation by DYRK1A increases its protein stability</title><author>Liu, Heng ; Wang, Ketao ; Chen, Shuai ; Sun, Qian ; Zhang, Yuankai ; Chen, Long ; Sun, Xiulian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c791t-91200f340c7c45876977b89f46f19948b75c5c078bf77401c31efcc29efab4673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Motifs</topic><topic>Analysis</topic><topic>Biology and Life Sciences</topic><topic>Cancer</topic><topic>Cytoplasm</topic><topic>Down syndrome</topic><topic>Drosophila</topic><topic>Dyrk Kinases</topic><topic>Genetic aspects</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Immune response</topic><topic>Immunology</topic><topic>Insects</topic><topic>Kinases</topic><topic>Lymphocytes</topic><topic>Medicine and Health Sciences</topic><topic>Monoclonal antibodies</topic><topic>NFATC Transcription Factors - 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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>Liu, Heng</au><au>Wang, Ketao</au><au>Chen, Shuai</au><au>Sun, Qian</au><au>Zhang, Yuankai</au><au>Chen, Long</au><au>Sun, Xiulian</au><au>Reddy, Sakamuri V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NFATc1 phosphorylation by DYRK1A increases its protein stability</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2017-02-24</date><risdate>2017</risdate><volume>12</volume><issue>2</issue><spage>e0172985</spage><epage>e0172985</epage><pages>e0172985-e0172985</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>NFATs are transcription factors involved in immune activation and tumor progression. Previous reports showed that DYRK1A suppressed NFATc2 transcriptional activity through phosphorylation. Nonetheless, our results showed that DYRK1A increased NFATc1/αA protein level and subsequent transcriptional activity. DYRK1A phosphorylation of NFATc1/αA at S261, S278, S403 and S409 interfered with NFATc1 ubiquitination and ubiquitin-proteasome degradation. Our results imply that DYRK1A is a positive kinase in regulation of NFATc1.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>28235034</pmid><doi>10.1371/journal.pone.0172985</doi><tpages>e0172985</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Motifs Analysis Biology and Life Sciences Cancer Cytoplasm Down syndrome Drosophila Dyrk Kinases Genetic aspects HEK293 Cells Humans Immune response Immunology Insects Kinases Lymphocytes Medicine and Health Sciences Monoclonal antibodies NFATC Transcription Factors - metabolism Otolaryngology Phosphorylation Physical Sciences Physiological aspects Proteasome Endopeptidase Complex - metabolism Proteasomes Protein expression Protein Serine-Threonine Kinases - metabolism Protein Stability Protein-Tyrosine Kinases - metabolism Proteins Proteolysis Research and Analysis Methods T cells Transcription factors Ubiquitin Ubiquitination |
| title | NFATc1 phosphorylation by DYRK1A increases its protein stability |
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