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Human Prk Is a Conserved Protein Serine/Threonine Kinase Involved in Regulating M Phase Functions
Human prk encodes a novel protein serine/threonine kinase capable of strongly phosphorylating casein but not histone H1 in vitro. prk expression is tightly regulated at various levels during different stages of the cell cycle in lung fibroblasts. The Prk kinase activity is relatively low during mito...
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Published in: | The Journal of biological chemistry 1997-11, Vol.272 (45), p.28646-28651 |
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creator | Ouyang, Bin Pan, Huiqi Lu, Luo Li, Jian Stambrook, Peter Li, Bo Dai, Wei |
description | Human prk encodes a novel protein serine/threonine kinase capable of strongly phosphorylating casein but not histone H1 in vitro. prk expression is tightly regulated at various levels during different stages of the cell cycle in lung fibroblasts. The Prk kinase activity is relatively low during mitosis, G1, and G1/S, and peaks during late S and G2 stages of the cell cycle. Recombinant human Prk expressed through the baculoviral vector system is capable of phosphorylating Cdc25C, a positive regulator for the G2/M transition. Human prk shares significant sequence homology with Saccharomyces cerevisiae CDC5 and Drosophila melanogaster polo, both of which are essential for mitosis and meiosis. Full-length prk transcripts greatly potentiate progesterone-induced meiotic maturation of Xenopus laevisoocytes. On the other hand, antisense prk transcripts significantly delay and reduce the rate of oocyte maturation. When expressed in a CDC5 mutant strain of S. cerevisiae, human Prk, but not a deletional mutant protein, fully rescues the temperature-sensitive phenotype of the budding yeast. Taken together,prk may represent a new protein kinase, playing an important role in regulating the onset and/or progression of mitosis in mammalian cells. |
doi_str_mv | 10.1074/jbc.272.45.28646 |
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The Prk kinase activity is relatively low during mitosis, G1, and G1/S, and peaks during late S and G2 stages of the cell cycle. Recombinant human Prk expressed through the baculoviral vector system is capable of phosphorylating Cdc25C, a positive regulator for the G2/M transition. Human prk shares significant sequence homology with Saccharomyces cerevisiae CDC5 and Drosophila melanogaster polo, both of which are essential for mitosis and meiosis. Full-length prk transcripts greatly potentiate progesterone-induced meiotic maturation of Xenopus laevisoocytes. On the other hand, antisense prk transcripts significantly delay and reduce the rate of oocyte maturation. When expressed in a CDC5 mutant strain of S. cerevisiae, human Prk, but not a deletional mutant protein, fully rescues the temperature-sensitive phenotype of the budding yeast. Taken together,prk may represent a new protein kinase, playing an important role in regulating the onset and/or progression of mitosis in mammalian cells.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.272.45.28646</identifier><identifier>PMID: 9353331</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Caseins - metabolism ; cdc25 Phosphatases ; Cell Cycle Proteins - metabolism ; Cells, Cultured ; Cloning, Molecular ; DNA, Complementary - chemistry ; Down-Regulation ; Drosophila ; Fibroblasts - enzymology ; Humans ; Lung Neoplasms - enzymology ; Mice ; Mitosis ; Molecular Sequence Data ; Phosphorylation ; Protein Kinase C ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; RNA, Messenger - metabolism ; Xenopus laevis</subject><ispartof>The Journal of biological chemistry, 1997-11, Vol.272 (45), p.28646-28651</ispartof><rights>1997 © 1997 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-7926f4d01b708720ac5fba350453d5d80b430eb214fa29b85fd6c3fe04791c373</citedby><cites>FETCH-LOGICAL-c447t-7926f4d01b708720ac5fba350453d5d80b430eb214fa29b85fd6c3fe04791c373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0021925818387039$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3535,27903,27904,45759</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9353331$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ouyang, Bin</creatorcontrib><creatorcontrib>Pan, Huiqi</creatorcontrib><creatorcontrib>Lu, Luo</creatorcontrib><creatorcontrib>Li, Jian</creatorcontrib><creatorcontrib>Stambrook, Peter</creatorcontrib><creatorcontrib>Li, Bo</creatorcontrib><creatorcontrib>Dai, Wei</creatorcontrib><title>Human Prk Is a Conserved Protein Serine/Threonine Kinase Involved in Regulating M Phase Functions</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Human prk encodes a novel protein serine/threonine kinase capable of strongly phosphorylating casein but not histone H1 in vitro. prk expression is tightly regulated at various levels during different stages of the cell cycle in lung fibroblasts. The Prk kinase activity is relatively low during mitosis, G1, and G1/S, and peaks during late S and G2 stages of the cell cycle. Recombinant human Prk expressed through the baculoviral vector system is capable of phosphorylating Cdc25C, a positive regulator for the G2/M transition. Human prk shares significant sequence homology with Saccharomyces cerevisiae CDC5 and Drosophila melanogaster polo, both of which are essential for mitosis and meiosis. Full-length prk transcripts greatly potentiate progesterone-induced meiotic maturation of Xenopus laevisoocytes. On the other hand, antisense prk transcripts significantly delay and reduce the rate of oocyte maturation. When expressed in a CDC5 mutant strain of S. cerevisiae, human Prk, but not a deletional mutant protein, fully rescues the temperature-sensitive phenotype of the budding yeast. Taken together,prk may represent a new protein kinase, playing an important role in regulating the onset and/or progression of mitosis in mammalian cells.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Caseins - metabolism</subject><subject>cdc25 Phosphatases</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cells, Cultured</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - chemistry</subject><subject>Down-Regulation</subject><subject>Drosophila</subject><subject>Fibroblasts - enzymology</subject><subject>Humans</subject><subject>Lung Neoplasms - enzymology</subject><subject>Mice</subject><subject>Mitosis</subject><subject>Molecular Sequence Data</subject><subject>Phosphorylation</subject><subject>Protein Kinase C</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>Xenopus laevis</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNqFkM9rFDEYhoNU6lq991LIoXibbX5OZryVxdrFSkut4C1kMt_spM4kNZlZ8b836y4ehGIuCXmf7-XjQeiUkiUlSlw8NnbJFFsKuWRVKcoXaEFJxQsu6bcjtCCE0aJmsnqFXqf0SPIRNT1GxzWXnHO6QOZ6Ho3Hd_E7Xids8Cr4BHELbf4KEziPv0B0Hi4e-gjB5xf-5LxJgNd-G4YdmJl72MyDmZzf4M_4rt_FV7O3k8ttb9DLzgwJ3h7uE_T16sPD6rq4uf24Xl3eFFYINRWqZmUnWkIbRSrFiLGyawyXREjeyrYijeAEGkZFZ1jdVLJrS8s7IELV1HLFT9C7fe9TDD9mSJMeXbIwDMZDmJNWNa9KTvl_QVoyTkq1A8ketDGkFKHTT9GNJv7SlOidfp3166xfC6n_6M8jZ4fuuRmh_Ttw8J3z833eu03_00XQjQu2h_Hfmvd7DLKwrYOok3XgLbR5xE66De75HX4D4gifEQ</recordid><startdate>19971107</startdate><enddate>19971107</enddate><creator>Ouyang, Bin</creator><creator>Pan, Huiqi</creator><creator>Lu, Luo</creator><creator>Li, Jian</creator><creator>Stambrook, Peter</creator><creator>Li, Bo</creator><creator>Dai, Wei</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19971107</creationdate><title>Human Prk Is a Conserved Protein Serine/Threonine Kinase Involved in Regulating M Phase Functions</title><author>Ouyang, Bin ; Pan, Huiqi ; Lu, Luo ; Li, Jian ; Stambrook, Peter ; Li, Bo ; Dai, Wei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-7926f4d01b708720ac5fba350453d5d80b430eb214fa29b85fd6c3fe04791c373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Caseins - metabolism</topic><topic>cdc25 Phosphatases</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cells, Cultured</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - chemistry</topic><topic>Down-Regulation</topic><topic>Drosophila</topic><topic>Fibroblasts - enzymology</topic><topic>Humans</topic><topic>Lung Neoplasms - enzymology</topic><topic>Mice</topic><topic>Mitosis</topic><topic>Molecular Sequence Data</topic><topic>Phosphorylation</topic><topic>Protein Kinase C</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ouyang, Bin</creatorcontrib><creatorcontrib>Pan, Huiqi</creatorcontrib><creatorcontrib>Lu, Luo</creatorcontrib><creatorcontrib>Li, Jian</creatorcontrib><creatorcontrib>Stambrook, Peter</creatorcontrib><creatorcontrib>Li, Bo</creatorcontrib><creatorcontrib>Dai, Wei</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ouyang, Bin</au><au>Pan, Huiqi</au><au>Lu, Luo</au><au>Li, Jian</au><au>Stambrook, Peter</au><au>Li, Bo</au><au>Dai, Wei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Prk Is a Conserved Protein Serine/Threonine Kinase Involved in Regulating M Phase Functions</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1997-11-07</date><risdate>1997</risdate><volume>272</volume><issue>45</issue><spage>28646</spage><epage>28651</epage><pages>28646-28651</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Human prk encodes a novel protein serine/threonine kinase capable of strongly phosphorylating casein but not histone H1 in vitro. prk expression is tightly regulated at various levels during different stages of the cell cycle in lung fibroblasts. The Prk kinase activity is relatively low during mitosis, G1, and G1/S, and peaks during late S and G2 stages of the cell cycle. Recombinant human Prk expressed through the baculoviral vector system is capable of phosphorylating Cdc25C, a positive regulator for the G2/M transition. Human prk shares significant sequence homology with Saccharomyces cerevisiae CDC5 and Drosophila melanogaster polo, both of which are essential for mitosis and meiosis. Full-length prk transcripts greatly potentiate progesterone-induced meiotic maturation of Xenopus laevisoocytes. On the other hand, antisense prk transcripts significantly delay and reduce the rate of oocyte maturation. When expressed in a CDC5 mutant strain of S. cerevisiae, human Prk, but not a deletional mutant protein, fully rescues the temperature-sensitive phenotype of the budding yeast. 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subjects | Amino Acid Sequence Animals Caseins - metabolism cdc25 Phosphatases Cell Cycle Proteins - metabolism Cells, Cultured Cloning, Molecular DNA, Complementary - chemistry Down-Regulation Drosophila Fibroblasts - enzymology Humans Lung Neoplasms - enzymology Mice Mitosis Molecular Sequence Data Phosphorylation Protein Kinase C Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism RNA, Messenger - metabolism Xenopus laevis |
title | Human Prk Is a Conserved Protein Serine/Threonine Kinase Involved in Regulating M Phase Functions |
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