Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis
Cell morphogenesis is of fundamental significance in all eukaryotes for development, differentiation, and cell proliferation. In fission yeast, Drosophila Furry‐like Mor2 plays an essential role in cell morphogenesis in concert with the NDR/Tricornered kinase Orb6. Mutations of these genes result in...
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| Veröffentlicht in: | The EMBO journal 2005-09, Vol.24 (17), p.3012-3025 |
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| creator | Kanai, Muneyoshi Kume, Kazunori Miyahara, Kohji Sakai, Keisuke Nakamura, Keigo Leonhard, Klaus Wiley, David J Verde, Fulvia Toda, Takashi Hirata, Dai |
| description | Cell morphogenesis is of fundamental significance in all eukaryotes for development, differentiation, and cell proliferation. In fission yeast,
Drosophila
Furry‐like Mor2 plays an essential role in cell morphogenesis in concert with the NDR/Tricornered kinase Orb6. Mutations of these genes result in the loss of cell polarity. Here we show that the conserved proteins, MO25‐like Pmo25, GC kinase Nak1, Mor2, and Orb6, constitute a morphogenesis network that is important for polarity control and cell separation. Intriguingly, Pmo25 was localized at the mitotic spindle pole bodies (SPBs) and then underwent translocation to the dividing medial region upon cytokinesis. Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1. Pmo25 and Nak1 in turn were essential for Orb6 kinase activity. Further, the Pmo25 localization at the SPBs and the Nak1‐Orb6 kinase activities during interphase were under the control of the Cdc7 and Sid1 kinases in the septation initiation network (SIN), suggesting a functional linkage between SIN and the network for cell morphogenesis/separation following cytokinesis. |
| doi_str_mv | 10.1038/sj.emboj.7600782 |
| format | Article |
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Drosophila
Furry‐like Mor2 plays an essential role in cell morphogenesis in concert with the NDR/Tricornered kinase Orb6. Mutations of these genes result in the loss of cell polarity. Here we show that the conserved proteins, MO25‐like Pmo25, GC kinase Nak1, Mor2, and Orb6, constitute a morphogenesis network that is important for polarity control and cell separation. Intriguingly, Pmo25 was localized at the mitotic spindle pole bodies (SPBs) and then underwent translocation to the dividing medial region upon cytokinesis. Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1. Pmo25 and Nak1 in turn were essential for Orb6 kinase activity. Further, the Pmo25 localization at the SPBs and the Nak1‐Orb6 kinase activities during interphase were under the control of the Cdc7 and Sid1 kinases in the septation initiation network (SIN), suggesting a functional linkage between SIN and the network for cell morphogenesis/separation following cytokinesis.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/sj.emboj.7600782</identifier><identifier>PMID: 16096637</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; cell morphogenesis ; Cell Polarity ; Conserved Sequence ; Drosophila Proteins - genetics ; EMBO06 ; EMBO37 ; Microfilament Proteins - genetics ; Microfilament Proteins - metabolism ; Microtubules - physiology ; MO25 ; Mor2 ; Morphogenesis ; Mutation ; Protein Binding ; Protein Kinases - metabolism ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Schizosaccharomyces - growth & development ; Schizosaccharomyces - physiology ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; SIN ; SPB ; Spindle Apparatus - metabolism ; Translocation ; Yeasts</subject><ispartof>The EMBO journal, 2005-09, Vol.24 (17), p.3012-3025</ispartof><rights>European Molecular Biology Organization 2005</rights><rights>Copyright © 2005 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Sep 7, 2005</rights><rights>Copyright © 2005, European Molecular Biology Organization 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6702-2f5f496d39d67ea37bcc3710c59ac8698792895438f29f9219425c93f772081c3</citedby><cites>FETCH-LOGICAL-c6702-2f5f496d39d67ea37bcc3710c59ac8698792895438f29f9219425c93f772081c3</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/PMC1201359/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1201359/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,1414,1430,27907,27908,41103,42172,45557,45558,46392,46816,51559,53774,53776</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/sj.emboj.7600782$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16096637$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kanai, Muneyoshi</creatorcontrib><creatorcontrib>Kume, Kazunori</creatorcontrib><creatorcontrib>Miyahara, Kohji</creatorcontrib><creatorcontrib>Sakai, Keisuke</creatorcontrib><creatorcontrib>Nakamura, Keigo</creatorcontrib><creatorcontrib>Leonhard, Klaus</creatorcontrib><creatorcontrib>Wiley, David J</creatorcontrib><creatorcontrib>Verde, Fulvia</creatorcontrib><creatorcontrib>Toda, Takashi</creatorcontrib><creatorcontrib>Hirata, Dai</creatorcontrib><title>Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Cell morphogenesis is of fundamental significance in all eukaryotes for development, differentiation, and cell proliferation. In fission yeast,
Drosophila
Furry‐like Mor2 plays an essential role in cell morphogenesis in concert with the NDR/Tricornered kinase Orb6. Mutations of these genes result in the loss of cell polarity. Here we show that the conserved proteins, MO25‐like Pmo25, GC kinase Nak1, Mor2, and Orb6, constitute a morphogenesis network that is important for polarity control and cell separation. Intriguingly, Pmo25 was localized at the mitotic spindle pole bodies (SPBs) and then underwent translocation to the dividing medial region upon cytokinesis. Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1. Pmo25 and Nak1 in turn were essential for Orb6 kinase activity. Further, the Pmo25 localization at the SPBs and the Nak1‐Orb6 kinase activities during interphase were under the control of the Cdc7 and Sid1 kinases in the septation initiation network (SIN), suggesting a functional linkage between SIN and the network for cell morphogenesis/separation following cytokinesis.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>cell morphogenesis</subject><subject>Cell Polarity</subject><subject>Conserved Sequence</subject><subject>Drosophila Proteins - genetics</subject><subject>EMBO06</subject><subject>EMBO37</subject><subject>Microfilament Proteins - genetics</subject><subject>Microfilament Proteins - metabolism</subject><subject>Microtubules - physiology</subject><subject>MO25</subject><subject>Mor2</subject><subject>Morphogenesis</subject><subject>Mutation</subject><subject>Protein Binding</subject><subject>Protein Kinases - metabolism</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Schizosaccharomyces - growth & development</subject><subject>Schizosaccharomyces - physiology</subject><subject>Schizosaccharomyces pombe Proteins - genetics</subject><subject>Schizosaccharomyces pombe Proteins - metabolism</subject><subject>SIN</subject><subject>SPB</subject><subject>Spindle Apparatus - metabolism</subject><subject>Translocation</subject><subject>Yeasts</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkUtvEzEUhUcIRENhzwZksWA3wY_4tUGiUVMeKUXiJbGxHMeTOp0ZD74zQPj1TDpRUpBQV7Z0v3N8rk-WPSZ4TDBTL2A99tUirsdSYCwVvZONyETgnGLJ72YjTAXJJ0Tpo-wBwBpjzJUk97MjIrAWgslRZmcBIMQabbyFFp1fUI6aFFsfahQAldHZMvz2S2Rb9PHDCbL1EoFv2q66vvaIB_B1G2yJipiQ82WJqpiay7jytYcAD7N7hS3BP9qdx9nn2emn6et8fnH2ZvpqnjshMc1pwYuJFkuml0J6y-TCOSYJdlxbp4RWUlOl-YSpgupCU6InlDvNCikpVsSx4-zl4Nt0i8ovXR8q2dI0KVQ2bUy0wfw9qcOlWcUfhlBMGNe9wfOdQYrfOw-tqQJs97G1jx0YoTiXGKtbQSIFp1JuwWf_gOvYpbr_BUM078uhagvhAXIpAiRf7CMTbLYtG1ib65bNruVe8vTmqgfBrtYe0APwM5R-c6uhOT0_eXswJ4MWelm98ulG6P8HejJoatt2ye8fPMzzYR6g9b_2Y5uujJBMcvP1_Zl5N50zIb98MzP2B0cS30g</recordid><startdate>20050907</startdate><enddate>20050907</enddate><creator>Kanai, Muneyoshi</creator><creator>Kume, Kazunori</creator><creator>Miyahara, Kohji</creator><creator>Sakai, Keisuke</creator><creator>Nakamura, Keigo</creator><creator>Leonhard, Klaus</creator><creator>Wiley, David J</creator><creator>Verde, Fulvia</creator><creator>Toda, Takashi</creator><creator>Hirata, Dai</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>7QG</scope><scope>7QL</scope><scope>7QP</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>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>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</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>PCBAR</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>20050907</creationdate><title>Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis</title><author>Kanai, Muneyoshi ; Kume, Kazunori ; Miyahara, Kohji ; Sakai, Keisuke ; Nakamura, Keigo ; Leonhard, Klaus ; Wiley, David J ; Verde, Fulvia ; Toda, Takashi ; Hirata, Dai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6702-2f5f496d39d67ea37bcc3710c59ac8698792895438f29f9219425c93f772081c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>cell morphogenesis</topic><topic>Cell Polarity</topic><topic>Conserved Sequence</topic><topic>Drosophila Proteins - genetics</topic><topic>EMBO06</topic><topic>EMBO37</topic><topic>Microfilament Proteins - genetics</topic><topic>Microfilament Proteins - metabolism</topic><topic>Microtubules - physiology</topic><topic>MO25</topic><topic>Mor2</topic><topic>Morphogenesis</topic><topic>Mutation</topic><topic>Protein Binding</topic><topic>Protein Kinases - metabolism</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Schizosaccharomyces - growth & development</topic><topic>Schizosaccharomyces - physiology</topic><topic>Schizosaccharomyces pombe Proteins - genetics</topic><topic>Schizosaccharomyces pombe Proteins - metabolism</topic><topic>SIN</topic><topic>SPB</topic><topic>Spindle Apparatus - metabolism</topic><topic>Translocation</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kanai, Muneyoshi</creatorcontrib><creatorcontrib>Kume, Kazunori</creatorcontrib><creatorcontrib>Miyahara, Kohji</creatorcontrib><creatorcontrib>Sakai, Keisuke</creatorcontrib><creatorcontrib>Nakamura, Keigo</creatorcontrib><creatorcontrib>Leonhard, Klaus</creatorcontrib><creatorcontrib>Wiley, David J</creatorcontrib><creatorcontrib>Verde, Fulvia</creatorcontrib><creatorcontrib>Toda, Takashi</creatorcontrib><creatorcontrib>Hirata, Dai</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>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue 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>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 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 (ProQuest)</collection><collection>Earth, Atmospheric & Aquatic 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>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</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>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Kanai, Muneyoshi</au><au>Kume, Kazunori</au><au>Miyahara, Kohji</au><au>Sakai, Keisuke</au><au>Nakamura, Keigo</au><au>Leonhard, Klaus</au><au>Wiley, David J</au><au>Verde, Fulvia</au><au>Toda, Takashi</au><au>Hirata, Dai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2005-09-07</date><risdate>2005</risdate><volume>24</volume><issue>17</issue><spage>3012</spage><epage>3025</epage><pages>3012-3025</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Cell morphogenesis is of fundamental significance in all eukaryotes for development, differentiation, and cell proliferation. In fission yeast,
Drosophila
Furry‐like Mor2 plays an essential role in cell morphogenesis in concert with the NDR/Tricornered kinase Orb6. Mutations of these genes result in the loss of cell polarity. Here we show that the conserved proteins, MO25‐like Pmo25, GC kinase Nak1, Mor2, and Orb6, constitute a morphogenesis network that is important for polarity control and cell separation. Intriguingly, Pmo25 was localized at the mitotic spindle pole bodies (SPBs) and then underwent translocation to the dividing medial region upon cytokinesis. Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1. Pmo25 and Nak1 in turn were essential for Orb6 kinase activity. Further, the Pmo25 localization at the SPBs and the Nak1‐Orb6 kinase activities during interphase were under the control of the Cdc7 and Sid1 kinases in the septation initiation network (SIN), suggesting a functional linkage between SIN and the network for cell morphogenesis/separation following cytokinesis.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>16096637</pmid><doi>10.1038/sj.emboj.7600782</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Carrier Proteins - genetics Carrier Proteins - metabolism Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism cell morphogenesis Cell Polarity Conserved Sequence Drosophila Proteins - genetics EMBO06 EMBO37 Microfilament Proteins - genetics Microfilament Proteins - metabolism Microtubules - physiology MO25 Mor2 Morphogenesis Mutation Protein Binding Protein Kinases - metabolism Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Schizosaccharomyces - growth & development Schizosaccharomyces - physiology Schizosaccharomyces pombe Proteins - genetics Schizosaccharomyces pombe Proteins - metabolism SIN SPB Spindle Apparatus - metabolism Translocation Yeasts |
| title | Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis |
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