Human POGZ modulates dissociation of HP1[alpha] from mitotic chromosome arms through Aurora B activation
Heterochromatin protein 1 (HP1) has an essential role in heterochromatin formation and mitotic progression through its interaction with various proteins. We have identified a unique HP1alpha-binding protein, POGZ (pogo transposable element-derived protein with zinc finger domain), using an advanced...
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| Veröffentlicht in: | Nature cell biology 2010-07, Vol.12 (7), p.719 |
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| creator | Nozawa, Ryu-suke Nagao, Koji Masuda, Hiro-taka Iwasaki, Osamu Hirota, Toru Nozaki, Naohito Kimura, Hiroshi Obuse, Chikashi |
| description | Heterochromatin protein 1 (HP1) has an essential role in heterochromatin formation and mitotic progression through its interaction with various proteins. We have identified a unique HP1alpha-binding protein, POGZ (pogo transposable element-derived protein with zinc finger domain), using an advanced proteomics approach. Proteins generally interact with HP1 through a PxVxL (where x is any amino-acid residue) motif; however, POGZ was found to bind to HP1alpha through a zinc-finger-like motif. Binding by POGZ, mediated through its zinc-finger-like motif, competed with PxVxL proteins and destabilized the HP1alpha-chromatin interaction. Depletion experiments confirmed that the POGZ HP1-binding domain is essential for normal mitotic progression and dissociation of HP1alpha from mitotic chromosome arms. Furthermore, POGZ is required for the correct activation and dissociation of Aurora B kinase from chromosome arms during M phase. These results reveal POGZ as an essential protein that links HP1alpha dissociation with Aurora B kinase activation during mitosis. |
| doi_str_mv | 10.1038/ncb2075 |
| format | Article |
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We have identified a unique HP1alpha-binding protein, POGZ (pogo transposable element-derived protein with zinc finger domain), using an advanced proteomics approach. Proteins generally interact with HP1 through a PxVxL (where x is any amino-acid residue) motif; however, POGZ was found to bind to HP1alpha through a zinc-finger-like motif. Binding by POGZ, mediated through its zinc-finger-like motif, competed with PxVxL proteins and destabilized the HP1alpha-chromatin interaction. Depletion experiments confirmed that the POGZ HP1-binding domain is essential for normal mitotic progression and dissociation of HP1alpha from mitotic chromosome arms. Furthermore, POGZ is required for the correct activation and dissociation of Aurora B kinase from chromosome arms during M phase. These results reveal POGZ as an essential protein that links HP1alpha dissociation with Aurora B kinase activation during mitosis.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb2075</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Chromosomes ; Kinases ; Medical research ; Proteins ; Proteomics ; Standard scores ; Yeast ; Zinc</subject><ispartof>Nature cell biology, 2010-07, Vol.12 (7), p.719</ispartof><rights>Copyright Nature Publishing Group Jul 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Nozawa, Ryu-suke</creatorcontrib><creatorcontrib>Nagao, Koji</creatorcontrib><creatorcontrib>Masuda, Hiro-taka</creatorcontrib><creatorcontrib>Iwasaki, Osamu</creatorcontrib><creatorcontrib>Hirota, Toru</creatorcontrib><creatorcontrib>Nozaki, Naohito</creatorcontrib><creatorcontrib>Kimura, Hiroshi</creatorcontrib><creatorcontrib>Obuse, Chikashi</creatorcontrib><title>Human POGZ modulates dissociation of HP1[alpha] from mitotic chromosome arms through Aurora B activation</title><title>Nature cell biology</title><description>Heterochromatin protein 1 (HP1) has an essential role in heterochromatin formation and mitotic progression through its interaction with various proteins. 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These results reveal POGZ as an essential protein that links HP1alpha dissociation with Aurora B kinase activation during mitosis.</description><subject>Chromosomes</subject><subject>Kinases</subject><subject>Medical research</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Standard scores</subject><subject>Yeast</subject><subject>Zinc</subject><issn>1465-7392</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNjMFOwzAQRC1EJQpU_MKKe8BunLg50gqaGz1wAqFq6yaNqzhbvDbfT0B8QE8zT280Qtwp-aBkvngc7G4uTXEhpkqbMtOlqS5_e1lkJq_mV-Ka-Sil0lqaqejq5HGAzev6HTztU4-xYdg7ZrIOo6MBqIV6oz6wP3X4CW0gD95Fis6C7UYiJt8ABs8QR06HDp5SoICwBLTRff_d3IpJiz03s_-8Efcvz2-rOjsF-koNx-2RUhhGtS2MkZWWxSI_a_QDQZFMVw</recordid><startdate>20100701</startdate><enddate>20100701</enddate><creator>Nozawa, Ryu-suke</creator><creator>Nagao, Koji</creator><creator>Masuda, Hiro-taka</creator><creator>Iwasaki, Osamu</creator><creator>Hirota, Toru</creator><creator>Nozaki, Naohito</creator><creator>Kimura, Hiroshi</creator><creator>Obuse, Chikashi</creator><general>Nature Publishing Group</general><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>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></search><sort><creationdate>20100701</creationdate><title>Human POGZ modulates dissociation of HP1[alpha] from mitotic chromosome arms through Aurora B activation</title><author>Nozawa, Ryu-suke ; 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We have identified a unique HP1alpha-binding protein, POGZ (pogo transposable element-derived protein with zinc finger domain), using an advanced proteomics approach. Proteins generally interact with HP1 through a PxVxL (where x is any amino-acid residue) motif; however, POGZ was found to bind to HP1alpha through a zinc-finger-like motif. Binding by POGZ, mediated through its zinc-finger-like motif, competed with PxVxL proteins and destabilized the HP1alpha-chromatin interaction. Depletion experiments confirmed that the POGZ HP1-binding domain is essential for normal mitotic progression and dissociation of HP1alpha from mitotic chromosome arms. Furthermore, POGZ is required for the correct activation and dissociation of Aurora B kinase from chromosome arms during M phase. These results reveal POGZ as an essential protein that links HP1alpha dissociation with Aurora B kinase activation during mitosis.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><doi>10.1038/ncb2075</doi></addata></record> |
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| subjects | Chromosomes Kinases Medical research Proteins Proteomics Standard scores Yeast Zinc |
| title | Human POGZ modulates dissociation of HP1[alpha] from mitotic chromosome arms through Aurora B activation |
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