Phosphorylated HuR shuttles in cycles
HuR is a ubiquitous RNA-binding protein (RBP) that associates with many mRNAs encoding proliferative proteins. Although predominantly nuclear, HuR translocation to the cytoplasm is linked to its ability to stabilize target mRNAs and modulate their translation. We recently reported that HuR phosphory...
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| Veröffentlicht in: | Cell cycle (Georgetown, Tex.) Tex.), 2008-10, Vol.7 (20), p.3124-3126 |
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| creator | Kim, Hyeon Ho Gorospe, Myriam |
| description | HuR is a ubiquitous RNA-binding protein (RBP) that associates with many mRNAs encoding proliferative proteins. Although predominantly nuclear, HuR translocation to the cytoplasm is linked to its ability to stabilize target mRNAs and modulate their translation. We recently reported that HuR phosphorylation by Cdk1 at S202 (within the HuR hinge region that is necessary for nucleocytoplasmic shuttle) increases HuR association with 14-3-3 and contributes to its nuclear retention. In this issue of Cell Cycle we report that residue S242 also regulates HuRâÃ,€Ã,™s cytoplasmic localization, influences cyclin expression, and modulates cell proliferation. Together with evidence of other post-translational HuR modifications, we propose that HuR phosphorylation ensures the timely mobilization of HuR across the nuclear envelope. In turn, HuR helps to schedule gene expression programs in a cell cycle-dependent manner. |
| doi_str_mv | 10.4161/cc.7.20.6884 |
| format | Article |
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Although predominantly nuclear, HuR translocation to the cytoplasm is linked to its ability to stabilize target mRNAs and modulate their translation. We recently reported that HuR phosphorylation by Cdk1 at S202 (within the HuR hinge region that is necessary for nucleocytoplasmic shuttle) increases HuR association with 14-3-3 and contributes to its nuclear retention. In this issue of Cell Cycle we report that residue S242 also regulates HuRâÃ,€Ã,™s cytoplasmic localization, influences cyclin expression, and modulates cell proliferation. Together with evidence of other post-translational HuR modifications, we propose that HuR phosphorylation ensures the timely mobilization of HuR across the nuclear envelope. In turn, HuR helps to schedule gene expression programs in a cell cycle-dependent manner.</description><identifier>ISSN: 1538-4101</identifier><identifier>EISSN: 1551-4005</identifier><identifier>DOI: 10.4161/cc.7.20.6884</identifier><identifier>PMID: 18927508</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Active Transport, Cell Nucleus - physiology ; Amino Acid Sequence ; Animals ; Antigens, Surface - chemistry ; Antigens, Surface - genetics ; Antigens, Surface - metabolism ; Binding ; Biology ; Bioscience ; Calcium ; Cancer ; Cell ; Cell Cycle - physiology ; Cycle ; Cyclins - metabolism ; Cytoplasm - metabolism ; ELAV Proteins ; ELAV-Like Protein 1 ; Extra View ; Humans ; Landes ; Molecular Sequence Data ; Organogenesis ; Phosphorylation ; Protein Kinase C - metabolism ; Proteins ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism</subject><ispartof>Cell cycle (Georgetown, Tex.), 2008-10, Vol.7 (20), p.3124-3126</ispartof><rights>Copyright © 2008 Landes Bioscience 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-ca4a0ef910934a0fb3c50dd19a586fc42827b004c3fc72aefcf819a387824b2f3</citedby></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/18927508$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Hyeon Ho</creatorcontrib><creatorcontrib>Gorospe, Myriam</creatorcontrib><title>Phosphorylated HuR shuttles in cycles</title><title>Cell cycle (Georgetown, Tex.)</title><addtitle>Cell Cycle</addtitle><description>HuR is a ubiquitous RNA-binding protein (RBP) that associates with many mRNAs encoding proliferative proteins. Although predominantly nuclear, HuR translocation to the cytoplasm is linked to its ability to stabilize target mRNAs and modulate their translation. We recently reported that HuR phosphorylation by Cdk1 at S202 (within the HuR hinge region that is necessary for nucleocytoplasmic shuttle) increases HuR association with 14-3-3 and contributes to its nuclear retention. In this issue of Cell Cycle we report that residue S242 also regulates HuRâÃ,€Ã,™s cytoplasmic localization, influences cyclin expression, and modulates cell proliferation. Together with evidence of other post-translational HuR modifications, we propose that HuR phosphorylation ensures the timely mobilization of HuR across the nuclear envelope. In turn, HuR helps to schedule gene expression programs in a cell cycle-dependent manner.</description><subject>Active Transport, Cell Nucleus - physiology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, Surface - chemistry</subject><subject>Antigens, Surface - genetics</subject><subject>Antigens, Surface - metabolism</subject><subject>Binding</subject><subject>Biology</subject><subject>Bioscience</subject><subject>Calcium</subject><subject>Cancer</subject><subject>Cell</subject><subject>Cell Cycle - physiology</subject><subject>Cycle</subject><subject>Cyclins - metabolism</subject><subject>Cytoplasm - metabolism</subject><subject>ELAV Proteins</subject><subject>ELAV-Like Protein 1</subject><subject>Extra View</subject><subject>Humans</subject><subject>Landes</subject><subject>Molecular Sequence Data</subject><subject>Organogenesis</subject><subject>Phosphorylation</subject><subject>Protein Kinase C - metabolism</subject><subject>Proteins</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><issn>1538-4101</issn><issn>1551-4005</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkMFLwzAUh4Mobk5vnmUXPdktSdMmvQgy1AkDRfQc0tfERbpmJq2y_96MzangKT94X773-CF0SvCIkZyMAUZ8RPEoF4LtoT7JMpIwjLP9dU5FwggmPXQUwhvGVPCCHKIeEQXlGRZ9dP44d2E5d35Vq1ZXw2n3NAzzrm1rHYa2GcIKYjpGB0bVQZ9s3wF6ub15nkyT2cPd_eR6lgDjuE1AMYW1KQgu0phMmUKGq4oUKhO5AUYF5SXGDFIDnCptwIg4TAUXlJXUpAN0tfEuu3KhK9BN61Utl94ulF9Jp6z8O2nsXL66D0kzzqMkCi62Au_eOx1aubABdF2rRrsuyLzIeUa4iODlBgTvQvDa7JYQLNe9SgDJJcVy3WvEz34f9gNvi4zAeAPETZUOpXUBrG5A79DoU761sc5vJd_8sI1xfqE-na8r2apV7bzxqgEbZPrvMV9Ez5hS</recordid><startdate>20081015</startdate><enddate>20081015</enddate><creator>Kim, Hyeon Ho</creator><creator>Gorospe, Myriam</creator><general>Taylor & Francis</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20081015</creationdate><title>Phosphorylated HuR shuttles in cycles</title><author>Kim, Hyeon Ho ; Gorospe, Myriam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-ca4a0ef910934a0fb3c50dd19a586fc42827b004c3fc72aefcf819a387824b2f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Active Transport, Cell Nucleus - physiology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens, Surface - chemistry</topic><topic>Antigens, Surface - genetics</topic><topic>Antigens, Surface - metabolism</topic><topic>Binding</topic><topic>Biology</topic><topic>Bioscience</topic><topic>Calcium</topic><topic>Cancer</topic><topic>Cell</topic><topic>Cell Cycle - physiology</topic><topic>Cycle</topic><topic>Cyclins - metabolism</topic><topic>Cytoplasm - metabolism</topic><topic>ELAV Proteins</topic><topic>ELAV-Like Protein 1</topic><topic>Extra View</topic><topic>Humans</topic><topic>Landes</topic><topic>Molecular Sequence Data</topic><topic>Organogenesis</topic><topic>Phosphorylation</topic><topic>Protein Kinase C - metabolism</topic><topic>Proteins</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Hyeon Ho</creatorcontrib><creatorcontrib>Gorospe, Myriam</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell cycle (Georgetown, Tex.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Hyeon Ho</au><au>Gorospe, Myriam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylated HuR shuttles in cycles</atitle><jtitle>Cell cycle (Georgetown, Tex.)</jtitle><addtitle>Cell Cycle</addtitle><date>2008-10-15</date><risdate>2008</risdate><volume>7</volume><issue>20</issue><spage>3124</spage><epage>3126</epage><pages>3124-3126</pages><issn>1538-4101</issn><eissn>1551-4005</eissn><abstract>HuR is a ubiquitous RNA-binding protein (RBP) that associates with many mRNAs encoding proliferative proteins. 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| subjects | Active Transport, Cell Nucleus - physiology Amino Acid Sequence Animals Antigens, Surface - chemistry Antigens, Surface - genetics Antigens, Surface - metabolism Binding Biology Bioscience Calcium Cancer Cell Cell Cycle - physiology Cycle Cyclins - metabolism Cytoplasm - metabolism ELAV Proteins ELAV-Like Protein 1 Extra View Humans Landes Molecular Sequence Data Organogenesis Phosphorylation Protein Kinase C - metabolism Proteins RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism |
| title | Phosphorylated HuR shuttles in cycles |
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