Polo-Like Kinase Cdc5 Controls the Local Activation of Rho1 to Promote Cytokinesis
The links between the cell cycle machinery and the cytoskeletal proteins controlling cytokinesis are poorly understood. The small guanine nucleotide triphosphate (GTP)-binding protein RhoA stimulates type II myosin contractility and formin-dependent assembly of the cytokinetic actin contractile ring...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2006-07, Vol.313 (5783), p.108-111 |
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| creator | Yoshida, Satoshi Kono, Keiko Lowery, Drew M Bartolini, Sara Yaffe, Michael B Ohya, Yoshikazu Pellman, David |
| description | The links between the cell cycle machinery and the cytoskeletal proteins controlling cytokinesis are poorly understood. The small guanine nucleotide triphosphate (GTP)-binding protein RhoA stimulates type II myosin contractility and formin-dependent assembly of the cytokinetic actin contractile ring. We found that budding yeast Polo-like kinase Cdc5 controls the targeting and activation of Rho1 (RhoA) at the division site via Rho1 guanine nucleotide exchange factors. This role of Cdc5 (Polo-like kinase) in regulating Rho1 is likely to be relevant to cytokinesis and asymmetric cell division in other organisms. |
| doi_str_mv | 10.1126/science.1126747 |
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The small guanine nucleotide triphosphate (GTP)-binding protein RhoA stimulates type II myosin contractility and formin-dependent assembly of the cytokinetic actin contractile ring. We found that budding yeast Polo-like kinase Cdc5 controls the targeting and activation of Rho1 (RhoA) at the division site via Rho1 guanine nucleotide exchange factors. This role of Cdc5 (Polo-like kinase) in regulating Rho1 is likely to be relevant to cytokinesis and asymmetric cell division in other organisms.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1126747</identifier><identifier>PMID: 16763112</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Actins ; Actins - metabolism ; Amino Acid Motifs ; Anaphase ; Animal cells ; Cell cycle ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Cell division ; Cellular biology ; Cytokinesis ; Cytoskeleton ; Daughter cells ; enzyme activity ; Enzymes ; G-proteins ; Gene expression regulation ; Guanine Nucleotide Exchange Factors - chemistry ; Guanine Nucleotide Exchange Factors - genetics ; Guanine Nucleotide Exchange Factors - metabolism ; Guanosine Triphosphate - metabolism ; guanosinetriphosphatase ; Microfilament Proteins - metabolism ; Mitosis ; Mutation ; Phosphorylation ; Physiological regulation ; Protein Kinases - chemistry ; Protein Kinases - genetics ; Protein Kinases - metabolism ; protein phosphorylation ; protein-protein interactions ; Protein-Serine-Threonine Kinases ; Proteins ; Recombinant Fusion Proteins - metabolism ; rho GTP-Binding Proteins - metabolism ; Rho1 protein ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Saccharomycetales ; T lymphocytes ; Temperature ; Yeast ; Yeasts</subject><ispartof>Science (American Association for the Advancement of Science), 2006-07, Vol.313 (5783), p.108-111</ispartof><rights>Copyright 2006 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Jul 7, 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c566t-126d9acdc04893cabf93535f623e3aa5c2d28a637f53b4257e4d9c5823d6321f3</citedby><cites>FETCH-LOGICAL-c566t-126d9acdc04893cabf93535f623e3aa5c2d28a637f53b4257e4d9c5823d6321f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3846604$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3846604$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16763112$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoshida, Satoshi</creatorcontrib><creatorcontrib>Kono, Keiko</creatorcontrib><creatorcontrib>Lowery, Drew M</creatorcontrib><creatorcontrib>Bartolini, Sara</creatorcontrib><creatorcontrib>Yaffe, Michael B</creatorcontrib><creatorcontrib>Ohya, Yoshikazu</creatorcontrib><creatorcontrib>Pellman, David</creatorcontrib><title>Polo-Like Kinase Cdc5 Controls the Local Activation of Rho1 to Promote Cytokinesis</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The links between the cell cycle machinery and the cytoskeletal proteins controlling cytokinesis are poorly understood. The small guanine nucleotide triphosphate (GTP)-binding protein RhoA stimulates type II myosin contractility and formin-dependent assembly of the cytokinetic actin contractile ring. We found that budding yeast Polo-like kinase Cdc5 controls the targeting and activation of Rho1 (RhoA) at the division site via Rho1 guanine nucleotide exchange factors. 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| fulltext | fulltext |
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| ispartof | Science (American Association for the Advancement of Science), 2006-07, Vol.313 (5783), p.108-111 |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Actins Actins - metabolism Amino Acid Motifs Anaphase Animal cells Cell cycle Cell Cycle Proteins - chemistry Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Cell division Cellular biology Cytokinesis Cytoskeleton Daughter cells enzyme activity Enzymes G-proteins Gene expression regulation Guanine Nucleotide Exchange Factors - chemistry Guanine Nucleotide Exchange Factors - genetics Guanine Nucleotide Exchange Factors - metabolism Guanosine Triphosphate - metabolism guanosinetriphosphatase Microfilament Proteins - metabolism Mitosis Mutation Phosphorylation Physiological regulation Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - metabolism protein phosphorylation protein-protein interactions Protein-Serine-Threonine Kinases Proteins Recombinant Fusion Proteins - metabolism rho GTP-Binding Proteins - metabolism Rho1 protein Saccharomyces cerevisiae Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Saccharomycetales T lymphocytes Temperature Yeast Yeasts |
| title | Polo-Like Kinase Cdc5 Controls the Local Activation of Rho1 to Promote Cytokinesis |
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