YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation
YB-1 is a multifunctional DNA- and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. I...
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| Veröffentlicht in: | International journal of molecular sciences 2021-12, Vol.23 (1), p.428 |
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| creator | Sogorina, Ekaterina M Kim, Ekaterina R Sorokin, Alexey V Lyabin, Dmitry N Ovchinnikov, Lev P Mordovkina, Daria A Eliseeva, Irina A |
| description | YB-1 is a multifunctional DNA- and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import. |
| doi_str_mv | 10.3390/ijms23010428 |
| format | Article |
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YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms23010428</identifier><identifier>PMID: 35008856</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>AKT protein ; Amino Acid Sequence ; Amino acids ; Animals ; Cell differentiation ; Cell Nucleus - metabolism ; Cell proliferation ; Cytoplasm ; Damage localization ; Deoxyribonucleic acid ; DNA ; DNA damage ; HeLa Cells ; Humans ; Imports ; Insulin ; Kinases ; Localization ; Mice ; Multidrug resistance ; Mutation ; NIH 3T3 Cells ; Nuclear transport ; Phosphorylation ; Phosphoserine - metabolism ; Protein Binding ; Protein Transport ; Proteins ; Proto-Oncogene Proteins c-akt - metabolism ; RNA - metabolism ; RNA-binding protein ; Serine ; Serum ; Transcription ; Tumors ; Y-Box-Binding Protein 1 - chemistry ; Y-Box-Binding Protein 1 - metabolism</subject><ispartof>International journal of molecular sciences, 2021-12, Vol.23 (1), p.428</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-24b893ccaa9ff560ceedef8f2840812b65db68d33acf91a34c18e87513cf33253</citedby><cites>FETCH-LOGICAL-c412t-24b893ccaa9ff560ceedef8f2840812b65db68d33acf91a34c18e87513cf33253</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/PMC8745666/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8745666/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35008856$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sogorina, Ekaterina M</creatorcontrib><creatorcontrib>Kim, Ekaterina R</creatorcontrib><creatorcontrib>Sorokin, Alexey V</creatorcontrib><creatorcontrib>Lyabin, Dmitry N</creatorcontrib><creatorcontrib>Ovchinnikov, Lev P</creatorcontrib><creatorcontrib>Mordovkina, Daria A</creatorcontrib><creatorcontrib>Eliseeva, Irina A</creatorcontrib><title>YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>YB-1 is a multifunctional DNA- and RNA-binding protein involved in cell proliferation, differentiation, and migration. 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Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.</description><subject>AKT protein</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Cell differentiation</subject><subject>Cell Nucleus - metabolism</subject><subject>Cell proliferation</subject><subject>Cytoplasm</subject><subject>Damage localization</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA damage</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Imports</subject><subject>Insulin</subject><subject>Kinases</subject><subject>Localization</subject><subject>Mice</subject><subject>Multidrug resistance</subject><subject>Mutation</subject><subject>NIH 3T3 Cells</subject><subject>Nuclear transport</subject><subject>Phosphorylation</subject><subject>Phosphoserine - metabolism</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>RNA - metabolism</subject><subject>RNA-binding protein</subject><subject>Serine</subject><subject>Serum</subject><subject>Transcription</subject><subject>Tumors</subject><subject>Y-Box-Binding Protein 1 - chemistry</subject><subject>Y-Box-Binding Protein 1 - metabolism</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkd9LwzAQx4Mobk7ffJaCLz5YzY82TV4EHVMHQwXng08hTROb0TUzaYX999ZtjunBcQf3uS93fAE4RfCKEA6v7WweMIEIJpjtgT5KMI4hpNn-Tt8DRyHMIMQEp_wQ9EgKIWMp7YPR-12MopfShUXp_LKSjXV1JJvoVXtb6whDHo3r0ua2CdG4y6dWVVr6aOplHSqnVgvH4MDIKuiTTR2At_vRdPgYT54fxsPbSawShJsYJznjRCkpuTEphUrrQhtmMEsgQzinaZFTVhAileFIkkQhplmWIqIM6U4nA3Cz1l20-VwXSteNl5VYeDuXfimctOLvpLal-HBfgmVJSintBC42At59tjo0Ym6D0lUla-3aIDBFjENKuhiA83_ozLW-7t5bUZjwLEMddbmmlHcheG22xyAofvwRu_50-NnuA1v41xDyDQQ2ixc</recordid><startdate>20211231</startdate><enddate>20211231</enddate><creator>Sogorina, Ekaterina M</creator><creator>Kim, Ekaterina R</creator><creator>Sorokin, Alexey V</creator><creator>Lyabin, Dmitry N</creator><creator>Ovchinnikov, Lev P</creator><creator>Mordovkina, Daria A</creator><creator>Eliseeva, Irina A</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>PHGZM</scope><scope>PHGZT</scope><scope>PIMPY</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20211231</creationdate><title>YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation</title><author>Sogorina, Ekaterina M ; Kim, Ekaterina R ; Sorokin, Alexey V ; Lyabin, Dmitry N ; Ovchinnikov, Lev P ; Mordovkina, Daria A ; Eliseeva, Irina A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-24b893ccaa9ff560ceedef8f2840812b65db68d33acf91a34c18e87513cf33253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>AKT protein</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Cell differentiation</topic><topic>Cell Nucleus - metabolism</topic><topic>Cell proliferation</topic><topic>Cytoplasm</topic><topic>Damage localization</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA damage</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Imports</topic><topic>Insulin</topic><topic>Kinases</topic><topic>Localization</topic><topic>Mice</topic><topic>Multidrug resistance</topic><topic>Mutation</topic><topic>NIH 3T3 Cells</topic><topic>Nuclear transport</topic><topic>Phosphorylation</topic><topic>Phosphoserine - metabolism</topic><topic>Protein Binding</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>RNA - metabolism</topic><topic>RNA-binding protein</topic><topic>Serine</topic><topic>Serum</topic><topic>Transcription</topic><topic>Tumors</topic><topic>Y-Box-Binding Protein 1 - chemistry</topic><topic>Y-Box-Binding Protein 1 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sogorina, Ekaterina M</creatorcontrib><creatorcontrib>Kim, Ekaterina R</creatorcontrib><creatorcontrib>Sorokin, Alexey V</creatorcontrib><creatorcontrib>Lyabin, Dmitry N</creatorcontrib><creatorcontrib>Ovchinnikov, Lev P</creatorcontrib><creatorcontrib>Mordovkina, Daria A</creatorcontrib><creatorcontrib>Eliseeva, Irina A</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>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 Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</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>Research Library</collection><collection>Research Library (Corporate)</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</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><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sogorina, Ekaterina M</au><au>Kim, Ekaterina R</au><au>Sorokin, Alexey V</au><au>Lyabin, Dmitry N</au><au>Ovchinnikov, Lev P</au><au>Mordovkina, Daria A</au><au>Eliseeva, Irina A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2021-12-31</date><risdate>2021</risdate><volume>23</volume><issue>1</issue><spage>428</spage><pages>428-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>YB-1 is a multifunctional DNA- and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>35008856</pmid><doi>10.3390/ijms23010428</doi><oa>free_for_read</oa></addata></record> |
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| source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | AKT protein Amino Acid Sequence Amino acids Animals Cell differentiation Cell Nucleus - metabolism Cell proliferation Cytoplasm Damage localization Deoxyribonucleic acid DNA DNA damage HeLa Cells Humans Imports Insulin Kinases Localization Mice Multidrug resistance Mutation NIH 3T3 Cells Nuclear transport Phosphorylation Phosphoserine - metabolism Protein Binding Protein Transport Proteins Proto-Oncogene Proteins c-akt - metabolism RNA - metabolism RNA-binding protein Serine Serum Transcription Tumors Y-Box-Binding Protein 1 - chemistry Y-Box-Binding Protein 1 - metabolism |
| title | YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation |
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