Recruitment of the human Cdt1 replication licensing protein by the loop domain of Hec1 is required for stable kinetochore–microtubule attachment
Cdt1, a protein critical for replication origin licensing in G1 phase, is degraded during S phase but re-accumulates in G2 phase. We now demonstrate that human Cdt1 has a separable essential mitotic function. Cdt1 localizes to kinetochores during mitosis through interaction with the Hec1 component o...
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| Veröffentlicht in: | Nature cell biology 2012-06, Vol.14 (6), p.593-603 |
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| creator | Varma, Dileep Chandrasekaran, Srikripa Sundin, Lynsie J. R. Reidy, Karen T. Wan, Xiaohu Chasse, Dawn A. D. Nevis, Kathleen R. DeLuca, Jennifer G. Salmon, E. D. Cook, Jeanette Gowen |
| description | Cdt1, a protein critical for replication origin licensing in G1 phase, is degraded during S phase but re-accumulates in G2 phase. We now demonstrate that human Cdt1 has a separable essential mitotic function. Cdt1 localizes to kinetochores during mitosis through interaction with the Hec1 component of the Ndc80 complex. G2-specific depletion of Cdt1 arrests cells in late prometaphase owing to abnormally unstable kinetochore–microtubule (kMT) attachments and Mad1-dependent spindle-assembly-checkpoint activity. Cdt1 binds a unique loop extending from the rod domain of Hec1 that we show is also required for kMT attachment. Mutation of the loop domain prevents Cdt1 kinetochore localization and arrests cells in prometaphase. Super-resolution fluorescence microscopy indicates that Cdt1 binding to the Hec1 loop domain promotes a microtubule-dependent conformational change in the Ndc80 complex
in vivo
. These results support the conclusion that Cdt1 binding to Hec1 is essential for an extended Ndc80 configuration and stable kMT attachment.
The replication origin licensing factor Cdt1 is now demonstrated to function at the kinetochore in mitosis. Cook, Salmon and colleagues show that Cdt1 binds to the loop domain of Hec1 in the Ndc80 kinetochore complex and stabilizes kinetochore–microtubule attachment. |
| doi_str_mv | 10.1038/ncb2489 |
| format | Article |
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in vivo
. These results support the conclusion that Cdt1 binding to Hec1 is essential for an extended Ndc80 configuration and stable kMT attachment.
The replication origin licensing factor Cdt1 is now demonstrated to function at the kinetochore in mitosis. Cook, Salmon and colleagues show that Cdt1 binds to the loop domain of Hec1 in the Ndc80 kinetochore complex and stabilizes kinetochore–microtubule attachment.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb2489</identifier><identifier>PMID: 22581055</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/337/641/151 ; 631/80/641/1655 ; Amino Acid Sequence ; Arrests ; Biomedical and Life Sciences ; Cancer Research ; Cell Biology ; Cell Cycle Checkpoints ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Cell division ; Developmental Biology ; DNA replication ; Fluorescence ; Fluorescence microscopy ; Genomes ; HeLa Cells ; Humans ; Kinetochores ; Kinetochores - chemistry ; Kinetochores - metabolism ; Licenses ; Licensing ; Life Sciences ; Microtubules ; Microtubules - chemistry ; Microtubules - metabolism ; Mitosis ; Molecular biology ; Molecular Sequence Data ; Mutation ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Physiological aspects ; Proteins ; Stem Cells</subject><ispartof>Nature cell biology, 2012-06, Vol.14 (6), p.593-603</ispartof><rights>Springer Nature Limited 2012</rights><rights>COPYRIGHT 2012 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jun 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c597t-9ccd75a87ebe1d7b14f56323ab3a6dc3895f51bced052e4f21955e37997a9b543</citedby><cites>FETCH-LOGICAL-c597t-9ccd75a87ebe1d7b14f56323ab3a6dc3895f51bced052e4f21955e37997a9b543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ncb2489$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ncb2489$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22581055$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Varma, Dileep</creatorcontrib><creatorcontrib>Chandrasekaran, Srikripa</creatorcontrib><creatorcontrib>Sundin, Lynsie J. R.</creatorcontrib><creatorcontrib>Reidy, Karen T.</creatorcontrib><creatorcontrib>Wan, Xiaohu</creatorcontrib><creatorcontrib>Chasse, Dawn A. D.</creatorcontrib><creatorcontrib>Nevis, Kathleen R.</creatorcontrib><creatorcontrib>DeLuca, Jennifer G.</creatorcontrib><creatorcontrib>Salmon, E. D.</creatorcontrib><creatorcontrib>Cook, Jeanette Gowen</creatorcontrib><title>Recruitment of the human Cdt1 replication licensing protein by the loop domain of Hec1 is required for stable kinetochore–microtubule attachment</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>Cdt1, a protein critical for replication origin licensing in G1 phase, is degraded during S phase but re-accumulates in G2 phase. We now demonstrate that human Cdt1 has a separable essential mitotic function. Cdt1 localizes to kinetochores during mitosis through interaction with the Hec1 component of the Ndc80 complex. G2-specific depletion of Cdt1 arrests cells in late prometaphase owing to abnormally unstable kinetochore–microtubule (kMT) attachments and Mad1-dependent spindle-assembly-checkpoint activity. Cdt1 binds a unique loop extending from the rod domain of Hec1 that we show is also required for kMT attachment. Mutation of the loop domain prevents Cdt1 kinetochore localization and arrests cells in prometaphase. Super-resolution fluorescence microscopy indicates that Cdt1 binding to the Hec1 loop domain promotes a microtubule-dependent conformational change in the Ndc80 complex
in vivo
. These results support the conclusion that Cdt1 binding to Hec1 is essential for an extended Ndc80 configuration and stable kMT attachment.
The replication origin licensing factor Cdt1 is now demonstrated to function at the kinetochore in mitosis. Cook, Salmon and colleagues show that Cdt1 binds to the loop domain of Hec1 in the Ndc80 kinetochore complex and stabilizes kinetochore–microtubule attachment.</description><subject>631/337/641/151</subject><subject>631/80/641/1655</subject><subject>Amino Acid Sequence</subject><subject>Arrests</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell Cycle Checkpoints</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell division</subject><subject>Developmental Biology</subject><subject>DNA replication</subject><subject>Fluorescence</subject><subject>Fluorescence microscopy</subject><subject>Genomes</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Kinetochores</subject><subject>Kinetochores - chemistry</subject><subject>Kinetochores - metabolism</subject><subject>Licenses</subject><subject>Licensing</subject><subject>Life Sciences</subject><subject>Microtubules</subject><subject>Microtubules - chemistry</subject><subject>Microtubules - metabolism</subject><subject>Mitosis</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Physiological aspects</subject><subject>Proteins</subject><subject>Stem Cells</subject><issn>1465-7392</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptks9u1DAQxiMEoqUg3gBZ4gAcUvw3ji9I1QpopUpIBc6W40x2XRJ7azuI3ngGeEOeBG-7lF2EfLA185vPns9TVU8JPiaYta-97Shv1b3qkHDZ1LyR6v7m3IhaMkUPqkcpXWJMOMfyYXVAqWgJFuKw-nEBNs4uT-AzCgPKK0CreTIeLfpMUIT16KzJLnhUDuCT80u0jiGD86i7vuHHENaoD5MpoSJxCpYgl0rt1ewi9GgIEaVsuhHQF-chB7sKEX59_zk5W5Tmbi4Zk7Oxq80zHlcPBjMmeLLdj6rP795-WpzW5x_eny1OzmsrlMy1sraXwrQSOiC97AgfRMMoMx0zTW9Zq8QgSGehx4ICHyhRQgCTSkmjOsHZUfXmVnc9dxP0pbkczajX0U0mXutgnN7PeLfSy_BVM9Y0mKsi8HIrEMPVDCnrySUL42g8hDlpgknLOKUtK-jzf9DLMEdf2ruhJJas2aGWZgTt_BDKvXYjqk-ookxy3NBCHf-HKquHYmjwMLgS3yt4tVdQmAzf8tLMKemzjxf77ItbtvxMShGGOz8I1ptR09tRK-SzXfvuuD-z9deeVFJ-CXG3532t32V83fk</recordid><startdate>20120601</startdate><enddate>20120601</enddate><creator>Varma, Dileep</creator><creator>Chandrasekaran, Srikripa</creator><creator>Sundin, Lynsie J. 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D.</creatorcontrib><creatorcontrib>Cook, Jeanette Gowen</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</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>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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</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>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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</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>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Varma, Dileep</au><au>Chandrasekaran, Srikripa</au><au>Sundin, Lynsie J. R.</au><au>Reidy, Karen T.</au><au>Wan, Xiaohu</au><au>Chasse, Dawn A. D.</au><au>Nevis, Kathleen R.</au><au>DeLuca, Jennifer G.</au><au>Salmon, E. D.</au><au>Cook, Jeanette Gowen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recruitment of the human Cdt1 replication licensing protein by the loop domain of Hec1 is required for stable kinetochore–microtubule attachment</atitle><jtitle>Nature cell biology</jtitle><stitle>Nat Cell Biol</stitle><addtitle>Nat Cell Biol</addtitle><date>2012-06-01</date><risdate>2012</risdate><volume>14</volume><issue>6</issue><spage>593</spage><epage>603</epage><pages>593-603</pages><issn>1465-7392</issn><eissn>1476-4679</eissn><abstract>Cdt1, a protein critical for replication origin licensing in G1 phase, is degraded during S phase but re-accumulates in G2 phase. We now demonstrate that human Cdt1 has a separable essential mitotic function. Cdt1 localizes to kinetochores during mitosis through interaction with the Hec1 component of the Ndc80 complex. G2-specific depletion of Cdt1 arrests cells in late prometaphase owing to abnormally unstable kinetochore–microtubule (kMT) attachments and Mad1-dependent spindle-assembly-checkpoint activity. Cdt1 binds a unique loop extending from the rod domain of Hec1 that we show is also required for kMT attachment. Mutation of the loop domain prevents Cdt1 kinetochore localization and arrests cells in prometaphase. Super-resolution fluorescence microscopy indicates that Cdt1 binding to the Hec1 loop domain promotes a microtubule-dependent conformational change in the Ndc80 complex
in vivo
. These results support the conclusion that Cdt1 binding to Hec1 is essential for an extended Ndc80 configuration and stable kMT attachment.
The replication origin licensing factor Cdt1 is now demonstrated to function at the kinetochore in mitosis. Cook, Salmon and colleagues show that Cdt1 binds to the loop domain of Hec1 in the Ndc80 kinetochore complex and stabilizes kinetochore–microtubule attachment.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>22581055</pmid><doi>10.1038/ncb2489</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nature cell biology, 2012-06, Vol.14 (6), p.593-603 |
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| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature |
| subjects | 631/337/641/151 631/80/641/1655 Amino Acid Sequence Arrests Biomedical and Life Sciences Cancer Research Cell Biology Cell Cycle Checkpoints Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Cell division Developmental Biology DNA replication Fluorescence Fluorescence microscopy Genomes HeLa Cells Humans Kinetochores Kinetochores - chemistry Kinetochores - metabolism Licenses Licensing Life Sciences Microtubules Microtubules - chemistry Microtubules - metabolism Mitosis Molecular biology Molecular Sequence Data Mutation Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Physiological aspects Proteins Stem Cells |
| title | Recruitment of the human Cdt1 replication licensing protein by the loop domain of Hec1 is required for stable kinetochore–microtubule attachment |
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