Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation
Tri-methylation of histone H3 lysine 9 is important for recruiting heterochromatin protein 1 (HP1) to discrete regions of the genome, thereby regulating gene expression, chromatin packaging and heterochromatin formation. Here we show that HP1alpha, -beta, and -gamma are released from chromatin durin...
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| Veröffentlicht in: | Nature 2005-12, Vol.438 (7071), p.1116-1122 |
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| container_title | Nature |
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| creator | Hunt, Donald F Ueberheide, Beatrix M Allis, C. David Tseng, Boo Shan Dormann, Holger L Shabanowitz, Jeffrey Fischle, Wolfgang Funabiki, Hironori Garcia, Benjamin A |
| description | Tri-methylation of histone H3 lysine 9 is important for recruiting heterochromatin protein 1 (HP1) to discrete regions of the genome, thereby regulating gene expression, chromatin packaging and heterochromatin formation. Here we show that HP1alpha, -beta, and -gamma are released from chromatin during the M phase of the cell cycle, even though tri-methylation levels of histone H3 lysine 9 remain unchanged. However, the additional, transient modification of histone H3 by phosphorylation of serine 10 next to the more stable methyl-lysine 9 mark is sufficient to eject HP1 proteins from their binding sites. Inhibition or depletion of the mitotic kinase Aurora B, which phosphorylates serine 10 on histone H3, causes retention of HP1 proteins on mitotic chromosomes, suggesting that H3 serine 10 phosphorylation is necessary for the dissociation of HP1 from chromatin in M phase. These findings establish a regulatory mechanism of protein-protein interactions, through a combinatorial readout of two adjacent post-translational modifications: a stable methylation and a dynamic phosphorylation mark. |
| doi_str_mv | 10.1038/nature04219 |
| format | Article |
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Inhibition or depletion of the mitotic kinase Aurora B, which phosphorylates serine 10 on histone H3, causes retention of HP1 proteins on mitotic chromosomes, suggesting that H3 serine 10 phosphorylation is necessary for the dissociation of HP1 from chromatin in M phase. These findings establish a regulatory mechanism of protein-protein interactions, through a combinatorial readout of two adjacent post-translational modifications: a stable methylation and a dynamic phosphorylation mark.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/nature04219</identifier><identifier>PMID: 16222246</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Animals ; Aurora Kinase B ; Aurora Kinases ; Binding sites ; Biological and medical sciences ; Chromatin ; Chromatin - metabolism ; Chromatin. Chromosome ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosomes ; Chromosomes, Human - metabolism ; Fundamental and applied biological sciences. Psychology ; Genomics ; HeLa Cells ; Histones - metabolism ; Humans ; Methylation ; Mitosis ; Molecular and cellular biology ; Molecular genetics ; Oocytes - metabolism ; Packaging ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases - antagonists & inhibitors ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; Retention ; Xenopus laevis</subject><ispartof>Nature, 2005-12, Vol.438 (7071), p.1116-1122</ispartof><rights>2006 INIST-CNRS</rights><rights>COPYRIGHT 2005 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Dec 22, 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c672t-f2765b63972143c26c5578404870019a0a5456d0c3d380a3a31759b5022972663</citedby><cites>FETCH-LOGICAL-c672t-f2765b63972143c26c5578404870019a0a5456d0c3d380a3a31759b5022972663</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,2728,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17380477$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16222246$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hunt, Donald F</creatorcontrib><creatorcontrib>Ueberheide, Beatrix M</creatorcontrib><creatorcontrib>Allis, C. 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However, the additional, transient modification of histone H3 by phosphorylation of serine 10 next to the more stable methyl-lysine 9 mark is sufficient to eject HP1 proteins from their binding sites. Inhibition or depletion of the mitotic kinase Aurora B, which phosphorylates serine 10 on histone H3, causes retention of HP1 proteins on mitotic chromosomes, suggesting that H3 serine 10 phosphorylation is necessary for the dissociation of HP1 from chromatin in M phase. These findings establish a regulatory mechanism of protein-protein interactions, through a combinatorial readout of two adjacent post-translational modifications: a stable methylation and a dynamic phosphorylation mark.</description><subject>Animals</subject><subject>Aurora Kinase B</subject><subject>Aurora Kinases</subject><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>Chromatin</subject><subject>Chromatin - metabolism</subject><subject>Chromatin. 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David</au><au>Tseng, Boo Shan</au><au>Dormann, Holger L</au><au>Shabanowitz, Jeffrey</au><au>Fischle, Wolfgang</au><au>Funabiki, Hironori</au><au>Garcia, Benjamin A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation</atitle><jtitle>Nature</jtitle><addtitle>Nature</addtitle><date>2005-12-22</date><risdate>2005</risdate><volume>438</volume><issue>7071</issue><spage>1116</spage><epage>1122</epage><pages>1116-1122</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><eissn>1476-4679</eissn><coden>NATUAS</coden><abstract>Tri-methylation of histone H3 lysine 9 is important for recruiting heterochromatin protein 1 (HP1) to discrete regions of the genome, thereby regulating gene expression, chromatin packaging and heterochromatin formation. Here we show that HP1alpha, -beta, and -gamma are released from chromatin during the M phase of the cell cycle, even though tri-methylation levels of histone H3 lysine 9 remain unchanged. However, the additional, transient modification of histone H3 by phosphorylation of serine 10 next to the more stable methyl-lysine 9 mark is sufficient to eject HP1 proteins from their binding sites. Inhibition or depletion of the mitotic kinase Aurora B, which phosphorylates serine 10 on histone H3, causes retention of HP1 proteins on mitotic chromosomes, suggesting that H3 serine 10 phosphorylation is necessary for the dissociation of HP1 from chromatin in M phase. 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| subjects | Animals Aurora Kinase B Aurora Kinases Binding sites Biological and medical sciences Chromatin Chromatin - metabolism Chromatin. Chromosome Chromosomal Proteins, Non-Histone - metabolism Chromosomes Chromosomes, Human - metabolism Fundamental and applied biological sciences. Psychology Genomics HeLa Cells Histones - metabolism Humans Methylation Mitosis Molecular and cellular biology Molecular genetics Oocytes - metabolism Packaging Phosphorylation Protein Binding Protein-Serine-Threonine Kinases - antagonists & inhibitors Protein-Serine-Threonine Kinases - metabolism Proteins Retention Xenopus laevis |
| title | Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation |
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