Phosphorylation of Mitotic Kinesin-like Protein 2 by Polo-like Kinase 1 Is Required for Cytokinesis
We have investigated the function of mitotic kinesin-like protein (MKlp) 2, a kinesin localized to the central spindle, and demonstrate that its depletion results in a failure of cleavage furrow ingression and cytokinesis, and disrupts localization of polo-like kinase 1 (Plk1). MKlp2 is a target for...
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| Veröffentlicht in: | The Journal of cell biology 2003-09, Vol.162 (5), p.863-875 |
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| container_title | The Journal of cell biology |
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| creator | Neef, Rüdiger Preisinger, Christian Sutcliffe, Josephine Kopajtich, Robert Nigg, Erich A. Mayer, Thomas U. Barr, Francis A. |
| description | We have investigated the function of mitotic kinesin-like protein (MKlp) 2, a kinesin localized to the central spindle, and demonstrate that its depletion results in a failure of cleavage furrow ingression and cytokinesis, and disrupts localization of polo-like kinase 1 (Plk1). MKlp2 is a target for Plk1, and phosphorylated MKlp2 binds to the polo box domain of Plk1. Plk1 also binds directly to microtubules and targets to the central spindle via its polo box domain, and this interaction controls the activity of Plk1 toward MKlp2. An antibody to the neck region of MKlp2 that prevents phosphorylation of MKlp2 by Plk1 causes a cytokinesis defect when introduced into cells. We propose that phosphorylation of MKlp2 by Plk1 is necessary for the spatial restriction of Plk1 to the central spindle during anaphase and telophase, and the complex of these two proteins is required for cytokinesis. |
| doi_str_mv | 10.1083/jcb.200306009 |
| format | Article |
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MKlp2 is a target for Plk1, and phosphorylated MKlp2 binds to the polo box domain of Plk1. Plk1 also binds directly to microtubules and targets to the central spindle via its polo box domain, and this interaction controls the activity of Plk1 toward MKlp2. An antibody to the neck region of MKlp2 that prevents phosphorylation of MKlp2 by Plk1 causes a cytokinesis defect when introduced into cells. We propose that phosphorylation of MKlp2 by Plk1 is necessary for the spatial restriction of Plk1 to the central spindle during anaphase and telophase, and the complex of these two proteins is required for cytokinesis.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200306009</identifier><identifier>PMID: 12939256</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Animal cells ; Antibodies ; Cell cycle ; Cell Cycle Proteins ; Cell division ; Cell Division - physiology ; Cells ; Cyclin B - metabolism ; Cytokines ; Cytokinesis ; HeLa Cells ; Humans ; Inhibitor of Apoptosis Proteins ; Kinesins - genetics ; Kinesins - metabolism ; Microtubule-Associated Proteins - metabolism ; Microtubules ; Microtubules - metabolism ; Mitotic spindle apparatus ; Neoplasm Proteins ; Phosphorus ; Phosphorylation ; Polo-Like Kinase 1 ; Protein Binding ; Protein Kinases - metabolism ; Protein Serine-Threonine Kinases ; Protein Structure, Tertiary ; Proto-Oncogene Proteins ; RNA, Small Interfering - metabolism ; Small interfering RNA ; Spindle Apparatus - metabolism ; Survivin ; Tubulin - metabolism</subject><ispartof>The Journal of cell biology, 2003-09, Vol.162 (5), p.863-875</ispartof><rights>Copyright 2003 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Sep 1, 2003</rights><rights>Copyright © 2003, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497t-26a4eeab5d157cc4155aa5eab21f974c130d80e58c70520034b37a2ff9d118203</citedby><cites>FETCH-LOGICAL-c497t-26a4eeab5d157cc4155aa5eab21f974c130d80e58c70520034b37a2ff9d118203</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12939256$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Neef, Rüdiger</creatorcontrib><creatorcontrib>Preisinger, Christian</creatorcontrib><creatorcontrib>Sutcliffe, Josephine</creatorcontrib><creatorcontrib>Kopajtich, Robert</creatorcontrib><creatorcontrib>Nigg, Erich A.</creatorcontrib><creatorcontrib>Mayer, Thomas U.</creatorcontrib><creatorcontrib>Barr, Francis A.</creatorcontrib><title>Phosphorylation of Mitotic Kinesin-like Protein 2 by Polo-like Kinase 1 Is Required for Cytokinesis</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>We have investigated the function of mitotic kinesin-like protein (MKlp) 2, a kinesin localized to the central spindle, and demonstrate that its depletion results in a failure of cleavage furrow ingression and cytokinesis, and disrupts localization of polo-like kinase 1 (Plk1). MKlp2 is a target for Plk1, and phosphorylated MKlp2 binds to the polo box domain of Plk1. Plk1 also binds directly to microtubules and targets to the central spindle via its polo box domain, and this interaction controls the activity of Plk1 toward MKlp2. An antibody to the neck region of MKlp2 that prevents phosphorylation of MKlp2 by Plk1 causes a cytokinesis defect when introduced into cells. We propose that phosphorylation of MKlp2 by Plk1 is necessary for the spatial restriction of Plk1 to the central spindle during anaphase and telophase, and the complex of these two proteins is required for cytokinesis.</description><subject>Animal cells</subject><subject>Antibodies</subject><subject>Cell cycle</subject><subject>Cell Cycle Proteins</subject><subject>Cell division</subject><subject>Cell Division - physiology</subject><subject>Cells</subject><subject>Cyclin B - metabolism</subject><subject>Cytokines</subject><subject>Cytokinesis</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Inhibitor of Apoptosis Proteins</subject><subject>Kinesins - genetics</subject><subject>Kinesins - metabolism</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Microtubules</subject><subject>Microtubules - metabolism</subject><subject>Mitotic spindle apparatus</subject><subject>Neoplasm Proteins</subject><subject>Phosphorus</subject><subject>Phosphorylation</subject><subject>Polo-Like Kinase 1</subject><subject>Protein Binding</subject><subject>Protein Kinases - metabolism</subject><subject>Protein Serine-Threonine Kinases</subject><subject>Protein Structure, Tertiary</subject><subject>Proto-Oncogene Proteins</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Small interfering RNA</subject><subject>Spindle Apparatus - metabolism</subject><subject>Survivin</subject><subject>Tubulin - metabolism</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1vEzEQhi0EoqFw5IaQxaG3LeOv9e4FCUUUKoqIEJwtr9dLnG52UtuLlH-PQ6IWOI008-iZGb2EvGRwyaARbzeuu-QAAmqA9hFZMCWhapiEx2QBwFnVKq7OyLOUNgAgtRRPyRnjrWi5qhfErdaYdmuM-9HmgBPFgX4JGXNw9HOYfApTNYZbT1cRsw8T5bTb0xWOeGwXxiZPGb1O9Ju_m0P0PR0w0uU-4-0fQXpOngx2TP7FqZ6TH1cfvi8_VTdfP14v399UTrY6V7y20nvbqZ4p7ZxkSlmrSoOzodXSMQF9A141ToM6vCw7oS0fhrZnrOEgzsm7o3c3d1vfOz_laEezi2Fr496gDebfyRTW5if-Mpxp3nBdBBcnQcS72adstiE5P4528jgno0XNudKigG_-Azc4x6k8d3CBbmUtC1QdIRcxpeiH-0sYmEN2pmRn7rMr_Ou_z3-gT2EV4NUR2KSM8WFel50MxG-5Gp5T</recordid><startdate>20030901</startdate><enddate>20030901</enddate><creator>Neef, Rüdiger</creator><creator>Preisinger, Christian</creator><creator>Sutcliffe, Josephine</creator><creator>Kopajtich, Robert</creator><creator>Nigg, Erich A.</creator><creator>Mayer, Thomas U.</creator><creator>Barr, Francis A.</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20030901</creationdate><title>Phosphorylation of Mitotic Kinesin-like Protein 2 by Polo-like Kinase 1 Is Required for Cytokinesis</title><author>Neef, Rüdiger ; Preisinger, Christian ; Sutcliffe, Josephine ; Kopajtich, Robert ; Nigg, Erich A. ; Mayer, Thomas U. ; Barr, Francis A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-26a4eeab5d157cc4155aa5eab21f974c130d80e58c70520034b37a2ff9d118203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animal cells</topic><topic>Antibodies</topic><topic>Cell cycle</topic><topic>Cell Cycle Proteins</topic><topic>Cell division</topic><topic>Cell Division - physiology</topic><topic>Cells</topic><topic>Cyclin B - metabolism</topic><topic>Cytokines</topic><topic>Cytokinesis</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Inhibitor of Apoptosis Proteins</topic><topic>Kinesins - genetics</topic><topic>Kinesins - metabolism</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Microtubules</topic><topic>Microtubules - metabolism</topic><topic>Mitotic spindle apparatus</topic><topic>Neoplasm Proteins</topic><topic>Phosphorus</topic><topic>Phosphorylation</topic><topic>Polo-Like Kinase 1</topic><topic>Protein Binding</topic><topic>Protein Kinases - metabolism</topic><topic>Protein Serine-Threonine Kinases</topic><topic>Protein Structure, Tertiary</topic><topic>Proto-Oncogene Proteins</topic><topic>RNA, Small Interfering - metabolism</topic><topic>Small interfering RNA</topic><topic>Spindle Apparatus - metabolism</topic><topic>Survivin</topic><topic>Tubulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Neef, Rüdiger</creatorcontrib><creatorcontrib>Preisinger, Christian</creatorcontrib><creatorcontrib>Sutcliffe, Josephine</creatorcontrib><creatorcontrib>Kopajtich, Robert</creatorcontrib><creatorcontrib>Nigg, Erich A.</creatorcontrib><creatorcontrib>Mayer, Thomas U.</creatorcontrib><creatorcontrib>Barr, Francis 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>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Neef, Rüdiger</au><au>Preisinger, Christian</au><au>Sutcliffe, Josephine</au><au>Kopajtich, Robert</au><au>Nigg, Erich A.</au><au>Mayer, Thomas U.</au><au>Barr, Francis A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of Mitotic Kinesin-like Protein 2 by Polo-like Kinase 1 Is Required for Cytokinesis</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2003-09-01</date><risdate>2003</risdate><volume>162</volume><issue>5</issue><spage>863</spage><epage>875</epage><pages>863-875</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>We have investigated the function of mitotic kinesin-like protein (MKlp) 2, a kinesin localized to the central spindle, and demonstrate that its depletion results in a failure of cleavage furrow ingression and cytokinesis, and disrupts localization of polo-like kinase 1 (Plk1). MKlp2 is a target for Plk1, and phosphorylated MKlp2 binds to the polo box domain of Plk1. Plk1 also binds directly to microtubules and targets to the central spindle via its polo box domain, and this interaction controls the activity of Plk1 toward MKlp2. An antibody to the neck region of MKlp2 that prevents phosphorylation of MKlp2 by Plk1 causes a cytokinesis defect when introduced into cells. We propose that phosphorylation of MKlp2 by Plk1 is necessary for the spatial restriction of Plk1 to the central spindle during anaphase and telophase, and the complex of these two proteins is required for cytokinesis.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>12939256</pmid><doi>10.1083/jcb.200306009</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animal cells Antibodies Cell cycle Cell Cycle Proteins Cell division Cell Division - physiology Cells Cyclin B - metabolism Cytokines Cytokinesis HeLa Cells Humans Inhibitor of Apoptosis Proteins Kinesins - genetics Kinesins - metabolism Microtubule-Associated Proteins - metabolism Microtubules Microtubules - metabolism Mitotic spindle apparatus Neoplasm Proteins Phosphorus Phosphorylation Polo-Like Kinase 1 Protein Binding Protein Kinases - metabolism Protein Serine-Threonine Kinases Protein Structure, Tertiary Proto-Oncogene Proteins RNA, Small Interfering - metabolism Small interfering RNA Spindle Apparatus - metabolism Survivin Tubulin - metabolism |
| title | Phosphorylation of Mitotic Kinesin-like Protein 2 by Polo-like Kinase 1 Is Required for Cytokinesis |
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