Peripheral Golgi Protein GRASP65 Is a Target of Mitotic Polo-Like Kinase (Plk) and Cdc2
Cell division is characterized by orchestrated events of chromosome segregation, distribution of cellular organelles, and the eventual partitioning and separation of the two daughter cells. Mitotic kinases, including polo-like kinases (Plk), influence multiple events in mitosis. In yeast two-hybrid...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-11, Vol.97 (23), p.12589-12594 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Lin, Chin-Yo Madsen, Matthew L. Yarm, Frederic R. Jang, Young-Joo Liu, Xiaoqi Erikson, Raymond L. |
| description | Cell division is characterized by orchestrated events of chromosome segregation, distribution of cellular organelles, and the eventual partitioning and separation of the two daughter cells. Mitotic kinases, including polo-like kinases (Plk), influence multiple events in mitosis. In yeast two-hybrid screens using mammalian Plk C-terminal domain baits, we have identified Golgi peripheral protein GRASP65 (Golgi reassembly stacking protein of 65 kDa) as a Plk-binding protein. GRASP65 appears to function in the postmitotic reassembly of Golgi stacks. In this report we demonstrate binding between Plk and GRASP65 and provide in vitro and in vivo evidence that Plk is a GRASP65 kinase. Moreover, we show that Cdc2 can also phosphorylate GRASP65. In addition, we present data which support the observation that the conserved C terminus of Plk is important for its function. Deletion or frameshift mutations in the conserved C-terminal domain of Plk greatly diminish its ability to phosphorylate GRASP65. These and previous findings suggest that phosphorylation of Golgi components by mitotic kinases may regulate mechanisms of Golgi inheritance during cell division. |
| doi_str_mv | 10.1073/pnas.220423497 |
| format | Article |
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Mitotic kinases, including polo-like kinases (Plk), influence multiple events in mitosis. In yeast two-hybrid screens using mammalian Plk C-terminal domain baits, we have identified Golgi peripheral protein GRASP65 (Golgi reassembly stacking protein of 65 kDa) as a Plk-binding protein. GRASP65 appears to function in the postmitotic reassembly of Golgi stacks. In this report we demonstrate binding between Plk and GRASP65 and provide in vitro and in vivo evidence that Plk is a GRASP65 kinase. Moreover, we show that Cdc2 can also phosphorylate GRASP65. In addition, we present data which support the observation that the conserved C terminus of Plk is important for its function. Deletion or frameshift mutations in the conserved C-terminal domain of Plk greatly diminish its ability to phosphorylate GRASP65. These and previous findings suggest that phosphorylation of Golgi components by mitotic kinases may regulate mechanisms of Golgi inheritance during cell division.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.220423497</identifier><identifier>PMID: 11050165</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Animals ; Antibodies ; Autoradiography ; Biological Sciences ; CDC2 Protein Kinase - metabolism ; Cell Cycle Proteins ; Cell division ; Cell Line ; Cellular biology ; COS Cells ; Epitopes ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Gene Expression ; Gene expression regulation ; Golgi Apparatus - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mitosis ; Mutagenesis ; Oligopeptides ; Peptides ; Phosphorylation ; Product labeling ; Protein Kinases - genetics ; Protein Kinases - metabolism ; Protein-Serine-Threonine Kinases ; Proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Two-Hybrid System Techniques ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2000-11, Vol.97 (23), p.12589-12594</ispartof><rights>Copyright 1993-2000 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 7, 2000</rights><rights>Copyright © 2000, The National Academy of Sciences 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-1f74b9eeecf2dd1dd787e3be6896e4e7390a73b1ad1407bc034c049f1f5a52623</citedby><cites>FETCH-LOGICAL-c554t-1f74b9eeecf2dd1dd787e3be6896e4e7390a73b1ad1407bc034c049f1f5a52623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/97/23.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/123894$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/123894$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11050165$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lin, Chin-Yo</creatorcontrib><creatorcontrib>Madsen, Matthew L.</creatorcontrib><creatorcontrib>Yarm, Frederic R.</creatorcontrib><creatorcontrib>Jang, Young-Joo</creatorcontrib><creatorcontrib>Liu, Xiaoqi</creatorcontrib><creatorcontrib>Erikson, Raymond L.</creatorcontrib><title>Peripheral Golgi Protein GRASP65 Is a Target of Mitotic Polo-Like Kinase (Plk) and Cdc2</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Cell division is characterized by orchestrated events of chromosome segregation, distribution of cellular organelles, and the eventual partitioning and separation of the two daughter cells. Mitotic kinases, including polo-like kinases (Plk), influence multiple events in mitosis. In yeast two-hybrid screens using mammalian Plk C-terminal domain baits, we have identified Golgi peripheral protein GRASP65 (Golgi reassembly stacking protein of 65 kDa) as a Plk-binding protein. GRASP65 appears to function in the postmitotic reassembly of Golgi stacks. In this report we demonstrate binding between Plk and GRASP65 and provide in vitro and in vivo evidence that Plk is a GRASP65 kinase. Moreover, we show that Cdc2 can also phosphorylate GRASP65. In addition, we present data which support the observation that the conserved C terminus of Plk is important for its function. Deletion or frameshift mutations in the conserved C-terminal domain of Plk greatly diminish its ability to phosphorylate GRASP65. These and previous findings suggest that phosphorylation of Golgi components by mitotic kinases may regulate mechanisms of Golgi inheritance during cell division.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Autoradiography</subject><subject>Biological Sciences</subject><subject>CDC2 Protein Kinase - metabolism</subject><subject>Cell Cycle Proteins</subject><subject>Cell division</subject><subject>Cell Line</subject><subject>Cellular biology</subject><subject>COS Cells</subject><subject>Epitopes</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Gene Expression</subject><subject>Gene expression regulation</subject><subject>Golgi Apparatus - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mitosis</subject><subject>Mutagenesis</subject><subject>Oligopeptides</subject><subject>Peptides</subject><subject>Phosphorylation</subject><subject>Product labeling</subject><subject>Protein Kinases - genetics</subject><subject>Protein Kinases - metabolism</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Two-Hybrid System Techniques</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1vEzEQxS0EoqFw5YIEFqdy2DD-2LUtcakiCBVBrKCIo-XdnU2dbtfB6yD473GU0MKF0xzm92bezCPkKYM5AyVeb0c3zTkHyYU06h6ZMTCsqKSB-2QGwFWhJZcn5NE0bQDAlBoekhPGoARWlTPyrcbot1cY3UCXYVh7WseQ0I90-fn8S12V9GKijl66uMZEQ08_-hSSb2kdhlCs_DXSDz57QHpWD9evqBs7uuha_pg86N0w4ZNjPSVf3729XLwvVp-WF4vzVdGWpUwF65VsDCK2Pe861nVKKxQNVtpUKFEJA06JhrmOSVBNC0K2IE3P-tKVvOLilLw5zN3umhvsWhxTPsVuo79x8ZcNztt_O6O_suvwwzKtQWf5y6M8hu87nJLdhF0cs2PLgQkJXIsMzQ9QG8M0RexvxzOw-xTsPgV7m0IWPP_b1B1-fHsGzo7AXvinbZTlwjJeamP73TAk_Jky-uL_aCaeHYjNlEK8W8aFNlL8BgQioxs</recordid><startdate>20001107</startdate><enddate>20001107</enddate><creator>Lin, Chin-Yo</creator><creator>Madsen, Matthew L.</creator><creator>Yarm, Frederic R.</creator><creator>Jang, Young-Joo</creator><creator>Liu, Xiaoqi</creator><creator>Erikson, Raymond L.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><general>The National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20001107</creationdate><title>Peripheral Golgi Protein GRASP65 Is a Target of Mitotic Polo-Like Kinase (Plk) and Cdc2</title><author>Lin, Chin-Yo ; Madsen, Matthew L. ; Yarm, Frederic R. ; Jang, Young-Joo ; Liu, Xiaoqi ; Erikson, Raymond L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c554t-1f74b9eeecf2dd1dd787e3be6896e4e7390a73b1ad1407bc034c049f1f5a52623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Autoradiography</topic><topic>Biological Sciences</topic><topic>CDC2 Protein Kinase - metabolism</topic><topic>Cell Cycle Proteins</topic><topic>Cell division</topic><topic>Cell Line</topic><topic>Cellular biology</topic><topic>COS Cells</topic><topic>Epitopes</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Gene Expression</topic><topic>Gene expression regulation</topic><topic>Golgi Apparatus - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mitosis</topic><topic>Mutagenesis</topic><topic>Oligopeptides</topic><topic>Peptides</topic><topic>Phosphorylation</topic><topic>Product labeling</topic><topic>Protein Kinases - genetics</topic><topic>Protein Kinases - metabolism</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Two-Hybrid System Techniques</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lin, Chin-Yo</creatorcontrib><creatorcontrib>Madsen, Matthew L.</creatorcontrib><creatorcontrib>Yarm, Frederic R.</creatorcontrib><creatorcontrib>Jang, Young-Joo</creatorcontrib><creatorcontrib>Liu, Xiaoqi</creatorcontrib><creatorcontrib>Erikson, Raymond L.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lin, Chin-Yo</au><au>Madsen, Matthew L.</au><au>Yarm, Frederic R.</au><au>Jang, Young-Joo</au><au>Liu, Xiaoqi</au><au>Erikson, Raymond L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peripheral Golgi Protein GRASP65 Is a Target of Mitotic Polo-Like Kinase (Plk) and Cdc2</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2000-11-07</date><risdate>2000</risdate><volume>97</volume><issue>23</issue><spage>12589</spage><epage>12594</epage><pages>12589-12594</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Cell division is characterized by orchestrated events of chromosome segregation, distribution of cellular organelles, and the eventual partitioning and separation of the two daughter cells. Mitotic kinases, including polo-like kinases (Plk), influence multiple events in mitosis. In yeast two-hybrid screens using mammalian Plk C-terminal domain baits, we have identified Golgi peripheral protein GRASP65 (Golgi reassembly stacking protein of 65 kDa) as a Plk-binding protein. GRASP65 appears to function in the postmitotic reassembly of Golgi stacks. In this report we demonstrate binding between Plk and GRASP65 and provide in vitro and in vivo evidence that Plk is a GRASP65 kinase. Moreover, we show that Cdc2 can also phosphorylate GRASP65. In addition, we present data which support the observation that the conserved C terminus of Plk is important for its function. Deletion or frameshift mutations in the conserved C-terminal domain of Plk greatly diminish its ability to phosphorylate GRASP65. These and previous findings suggest that phosphorylation of Golgi components by mitotic kinases may regulate mechanisms of Golgi inheritance during cell division.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>11050165</pmid><doi>10.1073/pnas.220423497</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Antibodies Autoradiography Biological Sciences CDC2 Protein Kinase - metabolism Cell Cycle Proteins Cell division Cell Line Cellular biology COS Cells Epitopes Fungal Proteins - genetics Fungal Proteins - metabolism Gene Expression Gene expression regulation Golgi Apparatus - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Mitosis Mutagenesis Oligopeptides Peptides Phosphorylation Product labeling Protein Kinases - genetics Protein Kinases - metabolism Protein-Serine-Threonine Kinases Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Two-Hybrid System Techniques Yeasts |
| title | Peripheral Golgi Protein GRASP65 Is a Target of Mitotic Polo-Like Kinase (Plk) and Cdc2 |
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