PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody
A new link is reported between regulators of endosomal trafficking and cytokinesis. Production of the phosphoinositide lipid PI3P at the midbody triggers the KIF13A-mediated recruitment of the centrosomal proteins FYVE-CENT and TTC19 to the division site. TTC19 may in turn regulate abscission by con...
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| Veröffentlicht in: | Nature cell biology 2010-04, Vol.12 (4), p.362-371 |
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| creator | Sagona, Antonia P. Nezis, Ioannis P. Pedersen, Nina Marie Liestøl, Knut Poulton, John Rusten, Tor Erik Skotheim, Rolf I. Raiborg, Camilla Stenmark, Harald |
| description | A new link is reported between regulators of endosomal trafficking and cytokinesis. Production of the phosphoinositide lipid PI3P at the midbody triggers the KIF13A-mediated recruitment of the centrosomal proteins FYVE-CENT and TTC19 to the division site. TTC19 may in turn regulate abscission by control of the ESCRTIII complex.
Several subunits of the class III phosphatidylinositol-3-OH kinase (PI(3)K-III) complex are known as tumour suppressors. Here we uncover a function for this complex and its catalytic product phosphatidylinositol-3-phosphate (PtdIns(3)P) in cytokinesis. We show that PtdIns(3)P localizes to the midbody during cytokinesis and recruits a centrosomal protein, FYVE-CENT (ZFYVE26), and its binding partner TTC19, which in turn interacts with CHMP4B, an endosomal sorting complex required for transport (ESCRT)-III subunit implicated in the abscission step of cytokinesis. Translocation of FYVE-CENT and TTC19 from the centrosome to the midbody requires another FYVE-CENT-interacting protein, the microtubule motor KIF13A. Depletion of the VPS34 or Beclin 1 subunits of PI(3)K-III causes cytokinesis arrest and an increased number of binucleate and multinucleate cells, in a similar manner to the depletion of FYVE-CENT, KIF13A or TTC19. These results provide a mechanism for the translocation and docking of a cytokinesis regulatory machinery at the midbody. |
| doi_str_mv | 10.1038/ncb2036 |
| format | Article |
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Several subunits of the class III phosphatidylinositol-3-OH kinase (PI(3)K-III) complex are known as tumour suppressors. Here we uncover a function for this complex and its catalytic product phosphatidylinositol-3-phosphate (PtdIns(3)P) in cytokinesis. We show that PtdIns(3)P localizes to the midbody during cytokinesis and recruits a centrosomal protein, FYVE-CENT (ZFYVE26), and its binding partner TTC19, which in turn interacts with CHMP4B, an endosomal sorting complex required for transport (ESCRT)-III subunit implicated in the abscission step of cytokinesis. Translocation of FYVE-CENT and TTC19 from the centrosome to the midbody requires another FYVE-CENT-interacting protein, the microtubule motor KIF13A. Depletion of the VPS34 or Beclin 1 subunits of PI(3)K-III causes cytokinesis arrest and an increased number of binucleate and multinucleate cells, in a similar manner to the depletion of FYVE-CENT, KIF13A or TTC19. These results provide a mechanism for the translocation and docking of a cytokinesis regulatory machinery at the midbody.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb2036</identifier><identifier>PMID: 20208530</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/80/2023/2022 ; 631/80/641/2090 ; Abscission ; Animals ; Apoptosis Regulatory Proteins - metabolism ; Beclin-1 ; Biomedical and Life Sciences ; Biosensing Techniques ; Cancer ; Cancer Research ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Biology ; Cell Cycle ; Centrosome - enzymology ; Cytokinesis ; Developmental Biology ; Drosophila ; Drosophila Proteins - metabolism ; Endosomal Sorting Complexes Required for Transport - metabolism ; HeLa Cells ; Humans ; Kinases ; Kinesin - genetics ; Kinesin - metabolism ; Life Sciences ; Localization ; Membrane Proteins - metabolism ; Mice ; Microscopy, Fluorescence ; Mitosis ; Mutation ; Phosphatidylinositol 3-Kinases - genetics ; Phosphatidylinositol 3-Kinases - metabolism ; Phosphatidylinositol Phosphates - metabolism ; Protein Binding ; Protein Transport ; Proteins ; Recombinant Fusion Proteins - metabolism ; RNA Interference ; Signal Transduction ; Spindle Apparatus - enzymology ; Stem Cells ; Transfection ; Translocation</subject><ispartof>Nature cell biology, 2010-04, Vol.12 (4), p.362-371</ispartof><rights>Springer Nature Limited 2010</rights><rights>Copyright Nature Publishing Group Apr 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-d946b29a2ed86ea2f2ad7628cf507b11b2b060c3b9d77d22d45a3340cbb775793</citedby><cites>FETCH-LOGICAL-c406t-d946b29a2ed86ea2f2ad7628cf507b11b2b060c3b9d77d22d45a3340cbb775793</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/ncb2036$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ncb2036$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20208530$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sagona, Antonia P.</creatorcontrib><creatorcontrib>Nezis, Ioannis P.</creatorcontrib><creatorcontrib>Pedersen, Nina Marie</creatorcontrib><creatorcontrib>Liestøl, Knut</creatorcontrib><creatorcontrib>Poulton, John</creatorcontrib><creatorcontrib>Rusten, Tor Erik</creatorcontrib><creatorcontrib>Skotheim, Rolf I.</creatorcontrib><creatorcontrib>Raiborg, Camilla</creatorcontrib><creatorcontrib>Stenmark, Harald</creatorcontrib><title>PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>A new link is reported between regulators of endosomal trafficking and cytokinesis. Production of the phosphoinositide lipid PI3P at the midbody triggers the KIF13A-mediated recruitment of the centrosomal proteins FYVE-CENT and TTC19 to the division site. TTC19 may in turn regulate abscission by control of the ESCRTIII complex.
Several subunits of the class III phosphatidylinositol-3-OH kinase (PI(3)K-III) complex are known as tumour suppressors. Here we uncover a function for this complex and its catalytic product phosphatidylinositol-3-phosphate (PtdIns(3)P) in cytokinesis. We show that PtdIns(3)P localizes to the midbody during cytokinesis and recruits a centrosomal protein, FYVE-CENT (ZFYVE26), and its binding partner TTC19, which in turn interacts with CHMP4B, an endosomal sorting complex required for transport (ESCRT)-III subunit implicated in the abscission step of cytokinesis. Translocation of FYVE-CENT and TTC19 from the centrosome to the midbody requires another FYVE-CENT-interacting protein, the microtubule motor KIF13A. Depletion of the VPS34 or Beclin 1 subunits of PI(3)K-III causes cytokinesis arrest and an increased number of binucleate and multinucleate cells, in a similar manner to the depletion of FYVE-CENT, KIF13A or TTC19. These results provide a mechanism for the translocation and docking of a cytokinesis regulatory machinery at the midbody.</description><subject>631/80/2023/2022</subject><subject>631/80/641/2090</subject><subject>Abscission</subject><subject>Animals</subject><subject>Apoptosis Regulatory Proteins - metabolism</subject><subject>Beclin-1</subject><subject>Biomedical and Life Sciences</subject><subject>Biosensing Techniques</subject><subject>Cancer</subject><subject>Cancer Research</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Biology</subject><subject>Cell Cycle</subject><subject>Centrosome - enzymology</subject><subject>Cytokinesis</subject><subject>Developmental Biology</subject><subject>Drosophila</subject><subject>Drosophila Proteins - metabolism</subject><subject>Endosomal Sorting Complexes Required for Transport - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Kinases</subject><subject>Kinesin - genetics</subject><subject>Kinesin - metabolism</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Microscopy, Fluorescence</subject><subject>Mitosis</subject><subject>Mutation</subject><subject>Phosphatidylinositol 3-Kinases - genetics</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Phosphatidylinositol Phosphates - metabolism</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RNA Interference</subject><subject>Signal Transduction</subject><subject>Spindle Apparatus - enzymology</subject><subject>Stem Cells</subject><subject>Transfection</subject><subject>Translocation</subject><issn>1465-7392</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkE1PwkAQhjdGI4rGf2A2XsRDdb-62x4JASUS5YAmnpruR6FIu7i7PfDvLQEl4TSTzDPvTB4AbjB6xIgmT7WSBFF-Ai4wEzxiXKSn257HkaAp6YBL75cIYcaQOAcdgghKYoouQDYNelz7Hn2YQmXr4OzKQ7UJ9rusjS89DAtnm_kCvo5HmPajyugyD0ZDZ5RrylCZOkBbwNHX5zAaDN9mMNh2x8Cq1NLqzRU4K_KVN9f72gUfo-Fs8BJN3p_Hg_4kUgzxEOmUcUnSnBidcJOTguRacJKoIkZCYiyJRBwpKlMthCZEszinlCElpRCxSGkX3O9y187-NMaHrCq9MqtVXhvb-ExQmrBWBWvJuyNyaRtXt89lhCBMOaHkEKec9d6ZIlu7ssrdJsMo2xrP9sZb8nYf18hWzj_3p7gFejvAt6N6btzh3nHWLyNbhrY</recordid><startdate>20100401</startdate><enddate>20100401</enddate><creator>Sagona, Antonia P.</creator><creator>Nezis, Ioannis P.</creator><creator>Pedersen, Nina Marie</creator><creator>Liestøl, Knut</creator><creator>Poulton, John</creator><creator>Rusten, Tor Erik</creator><creator>Skotheim, Rolf I.</creator><creator>Raiborg, Camilla</creator><creator>Stenmark, Harald</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</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>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20100401</creationdate><title>PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody</title><author>Sagona, Antonia P. ; Nezis, Ioannis P. ; Pedersen, Nina Marie ; Liestøl, Knut ; Poulton, John ; Rusten, Tor Erik ; Skotheim, Rolf I. ; Raiborg, Camilla ; Stenmark, Harald</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-d946b29a2ed86ea2f2ad7628cf507b11b2b060c3b9d77d22d45a3340cbb775793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>631/80/2023/2022</topic><topic>631/80/641/2090</topic><topic>Abscission</topic><topic>Animals</topic><topic>Apoptosis Regulatory Proteins - 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Production of the phosphoinositide lipid PI3P at the midbody triggers the KIF13A-mediated recruitment of the centrosomal proteins FYVE-CENT and TTC19 to the division site. TTC19 may in turn regulate abscission by control of the ESCRTIII complex.
Several subunits of the class III phosphatidylinositol-3-OH kinase (PI(3)K-III) complex are known as tumour suppressors. Here we uncover a function for this complex and its catalytic product phosphatidylinositol-3-phosphate (PtdIns(3)P) in cytokinesis. We show that PtdIns(3)P localizes to the midbody during cytokinesis and recruits a centrosomal protein, FYVE-CENT (ZFYVE26), and its binding partner TTC19, which in turn interacts with CHMP4B, an endosomal sorting complex required for transport (ESCRT)-III subunit implicated in the abscission step of cytokinesis. Translocation of FYVE-CENT and TTC19 from the centrosome to the midbody requires another FYVE-CENT-interacting protein, the microtubule motor KIF13A. Depletion of the VPS34 or Beclin 1 subunits of PI(3)K-III causes cytokinesis arrest and an increased number of binucleate and multinucleate cells, in a similar manner to the depletion of FYVE-CENT, KIF13A or TTC19. These results provide a mechanism for the translocation and docking of a cytokinesis regulatory machinery at the midbody.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>20208530</pmid><doi>10.1038/ncb2036</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/80/2023/2022 631/80/641/2090 Abscission Animals Apoptosis Regulatory Proteins - metabolism Beclin-1 Biomedical and Life Sciences Biosensing Techniques Cancer Cancer Research Carrier Proteins - genetics Carrier Proteins - metabolism Cell Biology Cell Cycle Centrosome - enzymology Cytokinesis Developmental Biology Drosophila Drosophila Proteins - metabolism Endosomal Sorting Complexes Required for Transport - metabolism HeLa Cells Humans Kinases Kinesin - genetics Kinesin - metabolism Life Sciences Localization Membrane Proteins - metabolism Mice Microscopy, Fluorescence Mitosis Mutation Phosphatidylinositol 3-Kinases - genetics Phosphatidylinositol 3-Kinases - metabolism Phosphatidylinositol Phosphates - metabolism Protein Binding Protein Transport Proteins Recombinant Fusion Proteins - metabolism RNA Interference Signal Transduction Spindle Apparatus - enzymology Stem Cells Transfection Translocation |
| title | PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody |
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