Cell cycle regulation of central spindle assembly
The bipolar mitotic spindle is responsible for segregating sister chromatids at anaphase. Microtubule motor proteins generate spindle bipolarity and enable the spindle to perform mechanical work 1 . A major change in spindle architecture occurs at anaphase onset when central spindle assembly begins....
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| Veröffentlicht in: | Nature (London) 2004-08, Vol.430 (7002), p.908-913 |
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| creator | Mishima, Masanori Pavicic, Visnja Grüneberg, Ulrike Nigg, Erich A. Glotzer, Michael |
| description | The bipolar mitotic spindle is responsible for segregating sister chromatids at anaphase. Microtubule motor proteins generate spindle bipolarity and enable the spindle to perform mechanical work
1
. A major change in spindle architecture occurs at anaphase onset when central spindle assembly begins. This structure regulates the initiation of cytokinesis and is essential for its completion
2
. Central spindle assembly requires the centralspindlin complex composed of the
Caenorhabditis elegans
ZEN-4 (mammalian orthologue MKLP1) kinesin-like protein and the Rho family GAP CYK-4 (MgcRacGAP). Here we describe a regulatory mechanism that controls the timing of central spindle assembly. The mitotic kinase Cdk1/cyclin B phosphorylates the motor domain of ZEN-4 on a conserved site within a basic amino-terminal extension characteristic of the MKLP1 subfamily. Phosphorylation by Cdk1 diminishes the motor activity of ZEN-4 by reducing its affinity for microtubules. Preventing Cdk1 phosphorylation of ZEN-4/MKLP1 causes enhanced metaphase spindle localization and defects in chromosome segregation. Thus, phosphoregulation of the motor domain of MKLP1 kinesin ensures that central spindle assembly occurs at the appropriate time in the cell cycle and maintains genomic stability. |
| doi_str_mv | 10.1038/nature02767 |
| format | Article |
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1
. A major change in spindle architecture occurs at anaphase onset when central spindle assembly begins. This structure regulates the initiation of cytokinesis and is essential for its completion
2
. Central spindle assembly requires the centralspindlin complex composed of the
Caenorhabditis elegans
ZEN-4 (mammalian orthologue MKLP1) kinesin-like protein and the Rho family GAP CYK-4 (MgcRacGAP). Here we describe a regulatory mechanism that controls the timing of central spindle assembly. The mitotic kinase Cdk1/cyclin B phosphorylates the motor domain of ZEN-4 on a conserved site within a basic amino-terminal extension characteristic of the MKLP1 subfamily. Phosphorylation by Cdk1 diminishes the motor activity of ZEN-4 by reducing its affinity for microtubules. Preventing Cdk1 phosphorylation of ZEN-4/MKLP1 causes enhanced metaphase spindle localization and defects in chromosome segregation. Thus, phosphoregulation of the motor domain of MKLP1 kinesin ensures that central spindle assembly occurs at the appropriate time in the cell cycle and maintains genomic stability.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature02767</identifier><identifier>PMID: 15282614</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adenosine Triphosphatases - metabolism ; Amino Acid Sequence ; Anaphase ; Animals ; Biological and medical sciences ; Caenorhabditis elegans - cytology ; Caenorhabditis elegans - embryology ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - chemistry ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; CDC2 Protein Kinase - metabolism ; Cell cycle ; Cell Cycle - physiology ; Cell cycle, cell proliferation ; Cell division ; Cell physiology ; Cellular biology ; Chromosome Segregation ; Chromosomes ; Chromosomes - metabolism ; Conserved Sequence ; Cyclin B - metabolism ; Fundamental and applied biological sciences. Psychology ; Genomics ; HeLa Cells ; Humanities and Social Sciences ; Humans ; Kinesin - chemistry ; Kinesin - genetics ; Kinesin - metabolism ; letter ; Microtubule-Associated Proteins - metabolism ; Microtubules - metabolism ; Molecular and cellular biology ; Molecular Motor Proteins - chemistry ; Molecular Motor Proteins - genetics ; Molecular Motor Proteins - metabolism ; Molecular Sequence Data ; multidisciplinary ; Phosphoprotein Phosphatases - genetics ; Phosphoprotein Phosphatases - metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; Science ; Science (multidisciplinary) ; Spindle Apparatus - chemistry ; Spindle Apparatus - metabolism ; Time Factors ; Tubulin - metabolism</subject><ispartof>Nature (London), 2004-08, Vol.430 (7002), p.908-913</ispartof><rights>Macmillan Magazines Ltd. 2004</rights><rights>2005 INIST-CNRS</rights><rights>COPYRIGHT 2004 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. Aug 19, 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c579t-e3ef4b0a48c4614e041eab5d4ace319f7c6cfb0b6ca713680fe99c6f298b1cfb3</citedby><cites>FETCH-LOGICAL-c579t-e3ef4b0a48c4614e041eab5d4ace319f7c6cfb0b6ca713680fe99c6f298b1cfb3</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/nature02767$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nature02767$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16038044$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15282614$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mishima, Masanori</creatorcontrib><creatorcontrib>Pavicic, Visnja</creatorcontrib><creatorcontrib>Grüneberg, Ulrike</creatorcontrib><creatorcontrib>Nigg, Erich A.</creatorcontrib><creatorcontrib>Glotzer, Michael</creatorcontrib><title>Cell cycle regulation of central spindle assembly</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>The bipolar mitotic spindle is responsible for segregating sister chromatids at anaphase. Microtubule motor proteins generate spindle bipolarity and enable the spindle to perform mechanical work
1
. A major change in spindle architecture occurs at anaphase onset when central spindle assembly begins. This structure regulates the initiation of cytokinesis and is essential for its completion
2
. Central spindle assembly requires the centralspindlin complex composed of the
Caenorhabditis elegans
ZEN-4 (mammalian orthologue MKLP1) kinesin-like protein and the Rho family GAP CYK-4 (MgcRacGAP). Here we describe a regulatory mechanism that controls the timing of central spindle assembly. The mitotic kinase Cdk1/cyclin B phosphorylates the motor domain of ZEN-4 on a conserved site within a basic amino-terminal extension characteristic of the MKLP1 subfamily. Phosphorylation by Cdk1 diminishes the motor activity of ZEN-4 by reducing its affinity for microtubules. Preventing Cdk1 phosphorylation of ZEN-4/MKLP1 causes enhanced metaphase spindle localization and defects in chromosome segregation. Thus, phosphoregulation of the motor domain of MKLP1 kinesin ensures that central spindle assembly occurs at the appropriate time in the cell cycle and maintains genomic stability.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Anaphase</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Caenorhabditis elegans - cytology</subject><subject>Caenorhabditis elegans - embryology</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins - chemistry</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>CDC2 Protein Kinase - metabolism</subject><subject>Cell cycle</subject><subject>Cell Cycle - physiology</subject><subject>Cell cycle, cell proliferation</subject><subject>Cell division</subject><subject>Cell physiology</subject><subject>Cellular biology</subject><subject>Chromosome Segregation</subject><subject>Chromosomes</subject><subject>Chromosomes - metabolism</subject><subject>Conserved Sequence</subject><subject>Cyclin B - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genomics</subject><subject>HeLa Cells</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Kinesin - chemistry</subject><subject>Kinesin - genetics</subject><subject>Kinesin - metabolism</subject><subject>letter</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Microtubules - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular Motor Proteins - chemistry</subject><subject>Molecular Motor Proteins - genetics</subject><subject>Molecular Motor Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Phosphoprotein Phosphatases - genetics</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Spindle Apparatus - chemistry</subject><subject>Spindle Apparatus - metabolism</subject><subject>Time Factors</subject><subject>Tubulin - metabolism</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0t9r2zAQB3AxNtas29PehxmsMDZ3OuunH0vY2kJhsB_PQlZOxsWWU8mG5b-vQgJpRqDowaD7-M7-coS8B3oJlOlvwU5zRFopqV6QBXAlSy61ekkWlFa6pJrJM_ImpXtKqQDFX5MzEJWuJPAFgSX2feE2rsciYjv3durGUIy-cBimaPsirbuwylWbEg5Nv3lLXnnbJ3y3f56Tvz--_1nelHc_r2-XV3elE6qeSmToeUMt147nSUg5oG3EiluHDGqvnHS-oY10VgGTmnqsayd9VesGcoWdk4td33UcH2ZMkxm65PLX2oDjnIyUqlZCwrOQCYCchHgWgqYgqGAZfvwP3o9zDPlvTUW5qKBmW1TuUGt7NF3wY47LtRgwpzYG9F2-vgItq5rVXB2aHnm37h7MU3R5AuWzwqFzJ7t-Pnohmwn_Ta2dUzK3v38d2y876-KYUkRv1rEbbNwYoGa7SubJKmX9YR_C3Ay4Otj97mTwaQ9scrb30QbXpYOTuSPlW_d151IuhRbjIc1Tcx8B9F3c-Q</recordid><startdate>20040819</startdate><enddate>20040819</enddate><creator>Mishima, Masanori</creator><creator>Pavicic, Visnja</creator><creator>Grüneberg, Ulrike</creator><creator>Nigg, Erich A.</creator><creator>Glotzer, Michael</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>IQODW</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</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>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>7X8</scope></search><sort><creationdate>20040819</creationdate><title>Cell cycle regulation of central spindle assembly</title><author>Mishima, Masanori ; 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Psychology</topic><topic>Genomics</topic><topic>HeLa Cells</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Kinesin - chemistry</topic><topic>Kinesin - genetics</topic><topic>Kinesin - metabolism</topic><topic>letter</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Microtubules - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular Motor Proteins - chemistry</topic><topic>Molecular Motor Proteins - genetics</topic><topic>Molecular Motor Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>multidisciplinary</topic><topic>Phosphoprotein Phosphatases - genetics</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Spindle Apparatus - chemistry</topic><topic>Spindle Apparatus - metabolism</topic><topic>Time Factors</topic><topic>Tubulin - 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mishima, Masanori</au><au>Pavicic, Visnja</au><au>Grüneberg, Ulrike</au><au>Nigg, Erich A.</au><au>Glotzer, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cell cycle regulation of central spindle assembly</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2004-08-19</date><risdate>2004</risdate><volume>430</volume><issue>7002</issue><spage>908</spage><epage>913</epage><pages>908-913</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>The bipolar mitotic spindle is responsible for segregating sister chromatids at anaphase. Microtubule motor proteins generate spindle bipolarity and enable the spindle to perform mechanical work
1
. A major change in spindle architecture occurs at anaphase onset when central spindle assembly begins. This structure regulates the initiation of cytokinesis and is essential for its completion
2
. Central spindle assembly requires the centralspindlin complex composed of the
Caenorhabditis elegans
ZEN-4 (mammalian orthologue MKLP1) kinesin-like protein and the Rho family GAP CYK-4 (MgcRacGAP). Here we describe a regulatory mechanism that controls the timing of central spindle assembly. The mitotic kinase Cdk1/cyclin B phosphorylates the motor domain of ZEN-4 on a conserved site within a basic amino-terminal extension characteristic of the MKLP1 subfamily. Phosphorylation by Cdk1 diminishes the motor activity of ZEN-4 by reducing its affinity for microtubules. Preventing Cdk1 phosphorylation of ZEN-4/MKLP1 causes enhanced metaphase spindle localization and defects in chromosome segregation. Thus, phosphoregulation of the motor domain of MKLP1 kinesin ensures that central spindle assembly occurs at the appropriate time in the cell cycle and maintains genomic stability.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>15282614</pmid><doi>10.1038/nature02767</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 2004-08, Vol.430 (7002), p.908-913 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66797561 |
| source | MEDLINE; Nature; Springer Nature - Complete Springer Journals |
| subjects | Adenosine Triphosphatases - metabolism Amino Acid Sequence Anaphase Animals Biological and medical sciences Caenorhabditis elegans - cytology Caenorhabditis elegans - embryology Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - chemistry Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism CDC2 Protein Kinase - metabolism Cell cycle Cell Cycle - physiology Cell cycle, cell proliferation Cell division Cell physiology Cellular biology Chromosome Segregation Chromosomes Chromosomes - metabolism Conserved Sequence Cyclin B - metabolism Fundamental and applied biological sciences. Psychology Genomics HeLa Cells Humanities and Social Sciences Humans Kinesin - chemistry Kinesin - genetics Kinesin - metabolism letter Microtubule-Associated Proteins - metabolism Microtubules - metabolism Molecular and cellular biology Molecular Motor Proteins - chemistry Molecular Motor Proteins - genetics Molecular Motor Proteins - metabolism Molecular Sequence Data multidisciplinary Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism Phosphorylation Protein Binding Protein Structure, Tertiary Proteins Science Science (multidisciplinary) Spindle Apparatus - chemistry Spindle Apparatus - metabolism Time Factors Tubulin - metabolism |
| title | Cell cycle regulation of central spindle assembly |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T15%3A10%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cell%20cycle%20regulation%20of%20central%20spindle%20assembly&rft.jtitle=Nature%20(London)&rft.au=Mishima,%20Masanori&rft.date=2004-08-19&rft.volume=430&rft.issue=7002&rft.spage=908&rft.epage=913&rft.pages=908-913&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/nature02767&rft_dat=%3Cgale_proqu%3EA186293947%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204521933&rft_id=info:pmid/15282614&rft_galeid=A186293947&rfr_iscdi=true |