Shugoshin collaborates with protein phosphatase 2A to protect cohesin
Sister chromatid cohesion, mediated by a complex called cohesin, is crucial—particularly at centromeres—for proper chromosome segregation in mitosis and meiosis. In animal mitotic cells, phosphorylation of cohesin promotes its dissociation from chromosomes, but centromeric cohesin is protected by sh...
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| Veröffentlicht in: | Nature 2006-05, Vol.441 (7089), p.46-52 |
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| creator | Kitajima, Tomoya S. Sakuno, Takeshi Ishiguro, Kei-ichiro Iemura, Shun-ichiro Natsume, Tohru Kawashima, Shigehiro A. Watanabe, Yoshinori |
| description | Sister chromatid cohesion, mediated by a complex called cohesin, is crucial—particularly at centromeres—for proper chromosome segregation in mitosis and meiosis. In animal mitotic cells, phosphorylation of cohesin promotes its dissociation from chromosomes, but centromeric cohesin is protected by shugoshin until kinetochores are properly captured by the spindle microtubules. However, the mechanism of shugoshin-dependent protection of cohesin is unknown. Here we find a specific subtype of serine/threonine protein phosphatase 2A (PP2A) associating with human shugoshin. PP2A colocalizes with shugoshin at centromeres and is required for centromeric protection. Purified shugoshin complex has an ability to reverse the phosphorylation of cohesin
in vitro
, suggesting that dephosphorylation of cohesin is the mechanism of protection at centromeres. Meiotic shugoshin of fission yeast also associates with PP2A, with both proteins collaboratively protecting Rec8-containing cohesin at centromeres. Thus, we have revealed a conserved mechanism of centromeric protection of eukaryotic chromosomes in mitosis and meiosis. |
| doi_str_mv | 10.1038/nature04663 |
| format | Article |
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in vitro
, suggesting that dephosphorylation of cohesin is the mechanism of protection at centromeres. Meiotic shugoshin of fission yeast also associates with PP2A, with both proteins collaboratively protecting Rec8-containing cohesin at centromeres. Thus, we have revealed a conserved mechanism of centromeric protection of eukaryotic chromosomes in mitosis and meiosis.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/nature04663</identifier><identifier>PMID: 16541025</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Biological and medical sciences ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Cell cycle, cell proliferation ; Cell division ; Cell physiology ; Centromere - metabolism ; Chromatids - metabolism ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosome Pairing ; Chromosomes ; Cohesins ; Cohesion ; Fundamental and applied biological sciences. Psychology ; HeLa Cells ; Humanities and Social Sciences ; Humans ; Meiosis ; Mitosis ; Molecular and cellular biology ; Molecular biology ; multidisciplinary ; Multiprotein Complexes - genetics ; Multiprotein Complexes - metabolism ; Nuclear Proteins - metabolism ; Phosphoprotein Phosphatases - classification ; Phosphoprotein Phosphatases - genetics ; Phosphoprotein Phosphatases - metabolism ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 2 ; Proteins ; Schizosaccharomyces - cytology ; Schizosaccharomyces - genetics ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - metabolism ; Science ; Science (multidisciplinary) ; Yeasts</subject><ispartof>Nature, 2006-05, Vol.441 (7089), p.46-52</ispartof><rights>Springer Nature Limited 2006</rights><rights>2006 INIST-CNRS</rights><rights>COPYRIGHT 2006 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group May 4, 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c581t-95e292cbe42b92c90c338ca6d5b48ccd6ed2074d4384f4a538add19df528438e3</citedby><cites>FETCH-LOGICAL-c581t-95e292cbe42b92c90c338ca6d5b48ccd6ed2074d4384f4a538add19df528438e3</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/nature04663$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nature04663$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17712286$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16541025$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kitajima, Tomoya S.</creatorcontrib><creatorcontrib>Sakuno, Takeshi</creatorcontrib><creatorcontrib>Ishiguro, Kei-ichiro</creatorcontrib><creatorcontrib>Iemura, Shun-ichiro</creatorcontrib><creatorcontrib>Natsume, Tohru</creatorcontrib><creatorcontrib>Kawashima, Shigehiro A.</creatorcontrib><creatorcontrib>Watanabe, Yoshinori</creatorcontrib><title>Shugoshin collaborates with protein phosphatase 2A to protect cohesin</title><title>Nature</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>Sister chromatid cohesion, mediated by a complex called cohesin, is crucial—particularly at centromeres—for proper chromosome segregation in mitosis and meiosis. In animal mitotic cells, phosphorylation of cohesin promotes its dissociation from chromosomes, but centromeric cohesin is protected by shugoshin until kinetochores are properly captured by the spindle microtubules. However, the mechanism of shugoshin-dependent protection of cohesin is unknown. Here we find a specific subtype of serine/threonine protein phosphatase 2A (PP2A) associating with human shugoshin. PP2A colocalizes with shugoshin at centromeres and is required for centromeric protection. Purified shugoshin complex has an ability to reverse the phosphorylation of cohesin
in vitro
, suggesting that dephosphorylation of cohesin is the mechanism of protection at centromeres. Meiotic shugoshin of fission yeast also associates with PP2A, with both proteins collaboratively protecting Rec8-containing cohesin at centromeres. Thus, we have revealed a conserved mechanism of centromeric protection of eukaryotic chromosomes in mitosis and meiosis.</description><subject>Biological and medical sciences</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell cycle, cell proliferation</subject><subject>Cell division</subject><subject>Cell physiology</subject><subject>Centromere - metabolism</subject><subject>Chromatids - metabolism</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>Chromosome Pairing</subject><subject>Chromosomes</subject><subject>Cohesins</subject><subject>Cohesion</subject><subject>Fundamental and applied biological sciences. 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called cohesin, is crucial—particularly at centromeres—for proper chromosome segregation in mitosis and meiosis. In animal mitotic cells, phosphorylation of cohesin promotes its dissociation from chromosomes, but centromeric cohesin is protected by shugoshin until kinetochores are properly captured by the spindle microtubules. However, the mechanism of shugoshin-dependent protection of cohesin is unknown. Here we find a specific subtype of serine/threonine protein phosphatase 2A (PP2A) associating with human shugoshin. PP2A colocalizes with shugoshin at centromeres and is required for centromeric protection. Purified shugoshin complex has an ability to reverse the phosphorylation of cohesin
in vitro
, suggesting that dephosphorylation of cohesin is the mechanism of protection at centromeres. Meiotic shugoshin of fission yeast also associates with PP2A, with both proteins collaboratively protecting Rec8-containing cohesin at centromeres. Thus, we have revealed a conserved mechanism of centromeric protection of eukaryotic chromosomes in mitosis and meiosis.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>16541025</pmid><doi>10.1038/nature04663</doi><tpages>7</tpages></addata></record> |
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| ispartof | Nature, 2006-05, Vol.441 (7089), p.46-52 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
| subjects | Biological and medical sciences Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Cell cycle, cell proliferation Cell division Cell physiology Centromere - metabolism Chromatids - metabolism Chromosomal Proteins, Non-Histone - metabolism Chromosome Pairing Chromosomes Cohesins Cohesion Fundamental and applied biological sciences. Psychology HeLa Cells Humanities and Social Sciences Humans Meiosis Mitosis Molecular and cellular biology Molecular biology multidisciplinary Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Nuclear Proteins - metabolism Phosphoprotein Phosphatases - classification Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism Phosphoproteins - metabolism Phosphorylation Protein Binding Protein Phosphatase 2 Proteins Schizosaccharomyces - cytology Schizosaccharomyces - genetics Schizosaccharomyces - metabolism Schizosaccharomyces pombe Proteins - metabolism Science Science (multidisciplinary) Yeasts |
| title | Shugoshin collaborates with protein phosphatase 2A to protect cohesin |
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