Phosphoregulation of human Mps1 kinase
The dual-specificity protein kinase Mps1 (monopolar spindle 1) is a phosphoprotein required for error-free mitotic progression in eukaryotes. In the present study, we have investigated human Mps1 phosphorylation using combined mass spectrometric, mutational and phosphospecific antibody approaches. W...
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| Veröffentlicht in: | Biochemical journal 2009-01, Vol.417 (1), p.173-184 |
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| container_title | Biochemical journal |
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| creator | Tyler, Rebecca K Chu, Matthew L H Johnson, Hannah McKenzie, Edward A Gaskell, Simon J Eyers, Patrick A |
| description | The dual-specificity protein kinase Mps1 (monopolar spindle 1) is a phosphoprotein required for error-free mitotic progression in eukaryotes. In the present study, we have investigated human Mps1 phosphorylation using combined mass spectrometric, mutational and phosphospecific antibody approaches. We have identified 16 sites of Mps1 autophosphorylation in vitro, several of which are required for catalytic activity after expression in bacteria or in cultured human cells. Using novel phosphospecific antibodies, we show that endogenous Mps1 is phosphorylated on Thr(686) and Ser(821) during mitosis, and demonstrate that phosphorylated Mps1 localizes to the centrosomes of metaphase cells. Taken together, these results reveal the complexity of Mps1 regulation by multi-site phosphorylation, and demonstrate conclusively that phosphorylated Mps1 associates with centrosomes in mitotic human cells. |
| doi_str_mv | 10.1042/BJ20081310 |
| format | Article |
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In the present study, we have investigated human Mps1 phosphorylation using combined mass spectrometric, mutational and phosphospecific antibody approaches. We have identified 16 sites of Mps1 autophosphorylation in vitro, several of which are required for catalytic activity after expression in bacteria or in cultured human cells. Using novel phosphospecific antibodies, we show that endogenous Mps1 is phosphorylated on Thr(686) and Ser(821) during mitosis, and demonstrate that phosphorylated Mps1 localizes to the centrosomes of metaphase cells. Taken together, these results reveal the complexity of Mps1 regulation by multi-site phosphorylation, and demonstrate conclusively that phosphorylated Mps1 associates with centrosomes in mitotic human cells.</description><subject>Amino Acid Sequence</subject><subject>Catalytic Domain - genetics</subject><subject>Cell Cycle Proteins - chemistry</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Centrosome - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Mitosis</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Phosphorylation</subject><subject>Protein Structure, Secondary</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protein-Tyrosine Kinases</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tandem Mass Spectrometry</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM1Kw0AYRQdRbKxufADJqqAQ_eZ_sqxFrVLRha6H6WRiokkmZhrBtzehxa4uXA6Hy0XoHMM1BkZubp8IgMIUwwGKMJOQKEnUIYqACJYIIHiCTkL4BMAMGByjCVZCAZNphGavhQ9t4Tv30VdmU_om9nlc9LVp4uc24PirbExwp-goN1VwZ7ucovf7u7fFMlm9PDwu5qvEUs43yZpa6TKb0ZxYB8IwSVNBMsUdHmYAt0ZyzA0TVqhUcEw5EUMlU-MszTNHp-hy6y1MpduurE33q70p9XK-0mMH42zg6Q8e2NmWbTv_3buw0XUZrKsq0zjfBy2EJClNR_BqC9rOh9C5_N-MQY8P6v2DA3yxs_br2mV7dHcZ_QOKq2fu</recordid><startdate>20090101</startdate><enddate>20090101</enddate><creator>Tyler, Rebecca K</creator><creator>Chu, Matthew L H</creator><creator>Johnson, Hannah</creator><creator>McKenzie, Edward A</creator><creator>Gaskell, Simon J</creator><creator>Eyers, Patrick A</creator><general>Portland Press</general><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>7X8</scope><scope>1XC</scope><scope>VOOES</scope></search><sort><creationdate>20090101</creationdate><title>Phosphoregulation of human Mps1 kinase</title><author>Tyler, Rebecca K ; Chu, Matthew L H ; Johnson, Hannah ; McKenzie, Edward A ; Gaskell, Simon J ; Eyers, Patrick A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c355t-b3c7edcd3f2ce06a473962d85e160205ca7515a46c6896513526a7579aec3fde3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Catalytic Domain - genetics</topic><topic>Cell Cycle Proteins - chemistry</topic><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Centrosome - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Mitosis</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Phosphorylation</topic><topic>Protein Structure, Secondary</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protein-Tyrosine Kinases</topic><topic>Sequence Homology, Amino Acid</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tyler, Rebecca K</creatorcontrib><creatorcontrib>Chu, Matthew L H</creatorcontrib><creatorcontrib>Johnson, Hannah</creatorcontrib><creatorcontrib>McKenzie, Edward A</creatorcontrib><creatorcontrib>Gaskell, Simon J</creatorcontrib><creatorcontrib>Eyers, Patrick A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tyler, Rebecca K</au><au>Chu, Matthew L H</au><au>Johnson, Hannah</au><au>McKenzie, Edward A</au><au>Gaskell, Simon J</au><au>Eyers, Patrick A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphoregulation of human Mps1 kinase</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2009-01-01</date><risdate>2009</risdate><volume>417</volume><issue>1</issue><spage>173</spage><epage>184</epage><pages>173-184</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The dual-specificity protein kinase Mps1 (monopolar spindle 1) is a phosphoprotein required for error-free mitotic progression in eukaryotes. 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| ispartof | Biochemical journal, 2009-01, Vol.417 (1), p.173-184 |
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| subjects | Amino Acid Sequence Catalytic Domain - genetics Cell Cycle Proteins - chemistry Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Centrosome - metabolism HeLa Cells Humans Mitosis Models, Molecular Molecular Sequence Data Mutation Phosphorylation Protein Structure, Secondary Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Protein-Tyrosine Kinases Sequence Homology, Amino Acid Tandem Mass Spectrometry |
| title | Phosphoregulation of human Mps1 kinase |
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