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The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase
CLIP‐170/Restin belongs to a family of conserved microtubule (MT)‐associated proteins, which are important for MT organization and functions. CLIP‐170 is a phosphoprotein and phosphorylation is thought to regulate the binding of CLIP‐170 to MTs. However, little is known about the kinase(s) involved....
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Published in: | EMBO reports 2002-10, Vol.3 (10), p.988-994 |
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description | CLIP‐170/Restin belongs to a family of conserved microtubule (MT)‐associated proteins, which are important for MT organization and functions. CLIP‐170 is a phosphoprotein and phosphorylation is thought to regulate the binding of CLIP‐170 to MTs. However, little is known about the kinase(s) involved. In this study, we show that FKBP12‐rapamycin‐associated protein (FRAP, also called mTOR/RAFT) interacts with CLIP‐170. CLIP‐170 is phosphorylated
in vivo
at multiple sites, including rapamycin‐sensitive and ‐insensitive sites, and is phosphorylated by FRAP
in vitro
at the rapamycin‐sensitive sites. In addition, rapamycin inhibited the ability of CLIP‐170 to bind to MTs. Our observations suggest that multiple CLIP‐170 kinases are involved in positive and negative control of CLIP‐170, and FRAP is a CLIP‐170 kinase positively regulating the MT‐binding behavior of CLIP‐170. |
doi_str_mv | 10.1093/embo-reports/kvf197 |
format | article |
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in vivo
at multiple sites, including rapamycin‐sensitive and ‐insensitive sites, and is phosphorylated by FRAP
in vitro
at the rapamycin‐sensitive sites. In addition, rapamycin inhibited the ability of CLIP‐170 to bind to MTs. Our observations suggest that multiple CLIP‐170 kinases are involved in positive and negative control of CLIP‐170, and FRAP is a CLIP‐170 kinase positively regulating the MT‐binding behavior of CLIP‐170.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.1093/embo-reports/kvf197</identifier><identifier>PMID: 12231510</identifier><identifier>CODEN: ERMEAX</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Animals ; Binding Sites ; Carrier Proteins ; Cattle ; Cell Line ; HeLa Cells ; Humans ; Immunophilins - chemistry ; Immunophilins - physiology ; Microtubule-Associated Proteins - chemistry ; Microtubule-Associated Proteins - metabolism ; Models, Biological ; Neoplasm Proteins ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor) ; Protein Binding ; Protein Structure, Tertiary ; Scientific Report ; Sirolimus - pharmacology ; Time Factors ; TOR Serine-Threonine Kinases</subject><ispartof>EMBO reports, 2002-10, Vol.3 (10), p.988-994</ispartof><rights>European Molecular Biology Organization 2002</rights><rights>Copyright © 2002 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Oct 15, 2002</rights><rights>Copyright © 2002, European Molecular Biology Organization 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6491-91e959f2057e012535ebd79aa99490dbf086fed931b38760d51612f275ee4ccf3</citedby><cites>FETCH-LOGICAL-c6491-91e959f2057e012535ebd79aa99490dbf086fed931b38760d51612f275ee4ccf3</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/PMC1307618/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1307618/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12231510$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Choi, Jae H</creatorcontrib><creatorcontrib>Bertram, Paula G</creatorcontrib><creatorcontrib>Drenan, Ryan</creatorcontrib><creatorcontrib>Carvalho, John</creatorcontrib><creatorcontrib>Zhou, Heather H</creatorcontrib><creatorcontrib>Zheng, X F Steven</creatorcontrib><title>The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>CLIP‐170/Restin belongs to a family of conserved microtubule (MT)‐associated proteins, which are important for MT organization and functions. CLIP‐170 is a phosphoprotein and phosphorylation is thought to regulate the binding of CLIP‐170 to MTs. However, little is known about the kinase(s) involved. In this study, we show that FKBP12‐rapamycin‐associated protein (FRAP, also called mTOR/RAFT) interacts with CLIP‐170. CLIP‐170 is phosphorylated
in vivo
at multiple sites, including rapamycin‐sensitive and ‐insensitive sites, and is phosphorylated by FRAP
in vitro
at the rapamycin‐sensitive sites. In addition, rapamycin inhibited the ability of CLIP‐170 to bind to MTs. Our observations suggest that multiple CLIP‐170 kinases are involved in positive and negative control of CLIP‐170, and FRAP is a CLIP‐170 kinase positively regulating the MT‐binding behavior of CLIP‐170.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Carrier Proteins</subject><subject>Cattle</subject><subject>Cell Line</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Immunophilins - chemistry</subject><subject>Immunophilins - physiology</subject><subject>Microtubule-Associated Proteins - chemistry</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Models, Biological</subject><subject>Neoplasm Proteins</subject><subject>Phosphorylation</subject><subject>Phosphotransferases (Alcohol Group Acceptor)</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Scientific Report</subject><subject>Sirolimus - pharmacology</subject><subject>Time Factors</subject><subject>TOR Serine-Threonine Kinases</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqNkUFv1DAQhSMEoqXwC5BQxAHBIdRjx3F8qdSuuqXqAstqEYiL5SST1t0kDnZS2H9PVom2wKknjzTfe36jFwQvgbwHItkx1pmNHLbWdf54c1eCFI-CQ4gTGTEQ6eNpphS-HwTPvL8lhHAp0qfBAVDKgAM5DGbrGwznV2dLoJHTra63uWki7b3Nje6wCFtnOzRN-Ha-Ol2-C40PdThbXC4jECTcmEZ7fB48KXXl8cX0HgVf5-fr2Ydo8fnicna6iPIklhBJQMllSQkXSIByxjErhNRayliSIitJmpRYSAYZS0VCCg4J0JIKjhjnecmOgpPRt-2zGoscm87pSrXO1NptldVG_btpzI26tncKGBEJpIPBm8nA2Z89-k7VxudYVbpB23slKHAWMxjA1_-Bt7Z3zXCcoiTlkIqUDxAbodxZ7x2W-yRA1K4htWtITQ2psaFB9ervI-41UyUDkI7AL1Ph9iGe6vzj2Yoku9jxKPWDqrlGdx_7QZEa3fUO91_uWDf6RiNgfIe_93vtNioRTHD17dOFWv1YgaBXa_WF_QHU_s7k</recordid><startdate>200210</startdate><enddate>200210</enddate><creator>Choi, Jae H</creator><creator>Bertram, Paula G</creator><creator>Drenan, Ryan</creator><creator>Carvalho, John</creator><creator>Zhou, Heather H</creator><creator>Zheng, X F Steven</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><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>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200210</creationdate><title>The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase</title><author>Choi, Jae H ; Bertram, Paula G ; Drenan, Ryan ; Carvalho, John ; Zhou, Heather H ; Zheng, X F Steven</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6491-91e959f2057e012535ebd79aa99490dbf086fed931b38760d51612f275ee4ccf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Carrier Proteins</topic><topic>Cattle</topic><topic>Cell Line</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Immunophilins - chemistry</topic><topic>Immunophilins - physiology</topic><topic>Microtubule-Associated Proteins - chemistry</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Models, Biological</topic><topic>Neoplasm Proteins</topic><topic>Phosphorylation</topic><topic>Phosphotransferases (Alcohol Group Acceptor)</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Scientific Report</topic><topic>Sirolimus - pharmacology</topic><topic>Time Factors</topic><topic>TOR Serine-Threonine Kinases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Choi, Jae H</creatorcontrib><creatorcontrib>Bertram, Paula G</creatorcontrib><creatorcontrib>Drenan, Ryan</creatorcontrib><creatorcontrib>Carvalho, John</creatorcontrib><creatorcontrib>Zhou, Heather H</creatorcontrib><creatorcontrib>Zheng, X F Steven</creatorcontrib><collection>Istex</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</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)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest research library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</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 Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choi, Jae H</au><au>Bertram, Paula G</au><au>Drenan, Ryan</au><au>Carvalho, John</au><au>Zhou, Heather H</au><au>Zheng, X F Steven</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2002-10</date><risdate>2002</risdate><volume>3</volume><issue>10</issue><spage>988</spage><epage>994</epage><pages>988-994</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><coden>ERMEAX</coden><abstract>CLIP‐170/Restin belongs to a family of conserved microtubule (MT)‐associated proteins, which are important for MT organization and functions. CLIP‐170 is a phosphoprotein and phosphorylation is thought to regulate the binding of CLIP‐170 to MTs. However, little is known about the kinase(s) involved. In this study, we show that FKBP12‐rapamycin‐associated protein (FRAP, also called mTOR/RAFT) interacts with CLIP‐170. CLIP‐170 is phosphorylated
in vivo
at multiple sites, including rapamycin‐sensitive and ‐insensitive sites, and is phosphorylated by FRAP
in vitro
at the rapamycin‐sensitive sites. In addition, rapamycin inhibited the ability of CLIP‐170 to bind to MTs. Our observations suggest that multiple CLIP‐170 kinases are involved in positive and negative control of CLIP‐170, and FRAP is a CLIP‐170 kinase positively regulating the MT‐binding behavior of CLIP‐170.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12231510</pmid><doi>10.1093/embo-reports/kvf197</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Binding Sites Carrier Proteins Cattle Cell Line HeLa Cells Humans Immunophilins - chemistry Immunophilins - physiology Microtubule-Associated Proteins - chemistry Microtubule-Associated Proteins - metabolism Models, Biological Neoplasm Proteins Phosphorylation Phosphotransferases (Alcohol Group Acceptor) Protein Binding Protein Structure, Tertiary Scientific Report Sirolimus - pharmacology Time Factors TOR Serine-Threonine Kinases |
title | The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase |
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