Characterization of PDZ-Binding Kinase, a Mitotic Kinase
hDlg, the human homologue of the Drosophila Discs-large (Dlg) tumor suppressor protein, is known to interact with the tumor suppressor protein APC and the human papillomavirus E6 transforming protein. In a two-hybrid screen, we identified a 322-aa serine/threonine kinase that binds to the PDZ2 domai...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-05, Vol.97 (10), p.5167-5172 |
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description | hDlg, the human homologue of the Drosophila Discs-large (Dlg) tumor suppressor protein, is known to interact with the tumor suppressor protein APC and the human papillomavirus E6 transforming protein. In a two-hybrid screen, we identified a 322-aa serine/threonine kinase that binds to the PDZ2 domain of hDlg. The mRNA for this PDZ-binding kinase, or PBK, is most abundant in placenta and absent from adult brain tissue. The protein sequence of PBK has all the characteristic protein kinase subdomains and a C-terminal PDZ-binding T/SXV motif. In vitro, PBK binds specifically to PDZ2 of hDlg through its C-terminal T/SXV motif. PBK and hDlg are phosphorylated at mitosis in HeLa cells, and the mitotic phosphorylation of PBK is required for its kinase activity. In vitro, cdc2/cyclin B phosphorylates PBK. This evidence shows how PBK could link hDlg or other PDZ-containing proteins to signal transduction pathways regulating the cell cycle or cellular proliferation. |
doi_str_mv | 10.1073/pnas.090102397 |
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In a two-hybrid screen, we identified a 322-aa serine/threonine kinase that binds to the PDZ2 domain of hDlg. The mRNA for this PDZ-binding kinase, or PBK, is most abundant in placenta and absent from adult brain tissue. The protein sequence of PBK has all the characteristic protein kinase subdomains and a C-terminal PDZ-binding T/SXV motif. In vitro, PBK binds specifically to PDZ2 of hDlg through its C-terminal T/SXV motif. PBK and hDlg are phosphorylated at mitosis in HeLa cells, and the mitotic phosphorylation of PBK is required for its kinase activity. In vitro, cdc2/cyclin B phosphorylates PBK. This evidence shows how PBK could link hDlg or other PDZ-containing proteins to signal transduction pathways regulating the cell cycle or cellular proliferation.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.090102397</identifier><identifier>PMID: 10779557</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adaptor Proteins, Signal Transducing ; Adult ; Amino Acid Sequence ; Animals ; Antibodies ; APC protein ; Binding Sites ; Biochemistry ; Biological Sciences ; Brain - enzymology ; cdc2 protein ; Cell Cycle ; Cell Line ; Complementary DNA ; Discs Large Homolog 1 Protein ; Drosophila ; Drosophila - enzymology ; E6 protein ; Female ; Guanylate Kinases ; hDlg protein ; HeLa Cells ; Histones ; Humans ; Membrane Proteins ; Mice ; Mitogen-Activated Protein Kinase Kinases ; Mitosis ; Molecular Sequence Data ; Phosphatases ; Phosphorylation ; Placenta - enzymology ; Pregnancy ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; protein-serine/threonine kinase ; Proteins ; Proteins - chemistry ; Proteins - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Spodoptera ; Transfection ; Zebrafish</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2000-05, Vol.97 (10), p.5167-5172</ispartof><rights>Copyright 1993-2000 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences May 9, 2000</rights><rights>Copyright © The National Academy of Sciences 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c583t-e7da1031f1e6d3dc3fe1a13176edea36b2a7fc81b8032d03a035a85e1c1012603</citedby><cites>FETCH-LOGICAL-c583t-e7da1031f1e6d3dc3fe1a13176edea36b2a7fc81b8032d03a035a85e1c1012603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/97/10.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/122305$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/122305$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10779557$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gaudet, Suzanne</creatorcontrib><creatorcontrib>Branton, Daniel</creatorcontrib><creatorcontrib>Lue, Robert A.</creatorcontrib><title>Characterization of PDZ-Binding Kinase, a Mitotic Kinase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>hDlg, the human homologue of the Drosophila Discs-large (Dlg) tumor suppressor protein, is known to interact with the tumor suppressor protein APC and the human papillomavirus E6 transforming protein. In a two-hybrid screen, we identified a 322-aa serine/threonine kinase that binds to the PDZ2 domain of hDlg. The mRNA for this PDZ-binding kinase, or PBK, is most abundant in placenta and absent from adult brain tissue. The protein sequence of PBK has all the characteristic protein kinase subdomains and a C-terminal PDZ-binding T/SXV motif. In vitro, PBK binds specifically to PDZ2 of hDlg through its C-terminal T/SXV motif. PBK and hDlg are phosphorylated at mitosis in HeLa cells, and the mitotic phosphorylation of PBK is required for its kinase activity. In vitro, cdc2/cyclin B phosphorylates PBK. This evidence shows how PBK could link hDlg or other PDZ-containing proteins to signal transduction pathways regulating the cell cycle or cellular proliferation.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Adult</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>APC protein</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Brain - enzymology</subject><subject>cdc2 protein</subject><subject>Cell Cycle</subject><subject>Cell Line</subject><subject>Complementary DNA</subject><subject>Discs Large Homolog 1 Protein</subject><subject>Drosophila</subject><subject>Drosophila - enzymology</subject><subject>E6 protein</subject><subject>Female</subject><subject>Guanylate Kinases</subject><subject>hDlg protein</subject><subject>HeLa Cells</subject><subject>Histones</subject><subject>Humans</subject><subject>Membrane Proteins</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinase Kinases</subject><subject>Mitosis</subject><subject>Molecular Sequence Data</subject><subject>Phosphatases</subject><subject>Phosphorylation</subject><subject>Placenta - enzymology</subject><subject>Pregnancy</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>protein-serine/threonine kinase</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spodoptera</subject><subject>Transfection</subject><subject>Zebrafish</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>eNqFkb2P1DAQxS0E4paDlgYJRRTQkGXGE8eJRAPLpzgEBTQ0ltdx7rzKxnu2g4C_Hke7HAsFVCPN_N48jx9jdxGWCJKe7EYdl9ACAqdWXmMLhBbLumrhOlsAcFk2Fa9O2K0YNwDQigZuspMsla0QcsGa1YUO2iQb3A-dnB8L3xcfX3wpn7uxc-N58c5lB_u40MV7l3xy5tC5zW70eoj2zqGess-vXn5avSnPPrx-u3p2VhrRUCqt7DQCYY-27qgz1FvUSChr21lN9Zpr2ZsG1w0Q74A0kNCNsGgQkNdAp-zpfu9uWm9tZ-yYgh7ULritDt-V1079ORndhTr3XxXPp87yhwd58JeTjUltXTR2GPRo_RSVxOwj6_a_IEpBNSeZwQd_gRs_hTH_geKAJKtKiAwt95AJPsZg-6sHI6g5ODUHp66Cy4L7x2ce4fukjoBZ-GvcynmhwHoGHv0TUP00DMl-S5m8tyc3Mfnw24pzAkE_AUSrs8M</recordid><startdate>20000509</startdate><enddate>20000509</enddate><creator>Gaudet, Suzanne</creator><creator>Branton, Daniel</creator><creator>Lue, Robert A.</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000509</creationdate><title>Characterization of PDZ-Binding Kinase, a Mitotic Kinase</title><author>Gaudet, Suzanne ; Branton, Daniel ; Lue, Robert A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c583t-e7da1031f1e6d3dc3fe1a13176edea36b2a7fc81b8032d03a035a85e1c1012603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Adult</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>APC protein</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Brain - enzymology</topic><topic>cdc2 protein</topic><topic>Cell Cycle</topic><topic>Cell Line</topic><topic>Complementary DNA</topic><topic>Discs Large Homolog 1 Protein</topic><topic>Drosophila</topic><topic>Drosophila - enzymology</topic><topic>E6 protein</topic><topic>Female</topic><topic>Guanylate Kinases</topic><topic>hDlg protein</topic><topic>HeLa Cells</topic><topic>Histones</topic><topic>Humans</topic><topic>Membrane Proteins</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinase Kinases</topic><topic>Mitosis</topic><topic>Molecular Sequence Data</topic><topic>Phosphatases</topic><topic>Phosphorylation</topic><topic>Placenta - enzymology</topic><topic>Pregnancy</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>protein-serine/threonine kinase</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spodoptera</topic><topic>Transfection</topic><topic>Zebrafish</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gaudet, Suzanne</creatorcontrib><creatorcontrib>Branton, Daniel</creatorcontrib><creatorcontrib>Lue, Robert 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>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>MEDLINE - Academic</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>Gaudet, Suzanne</au><au>Branton, Daniel</au><au>Lue, Robert A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of PDZ-Binding Kinase, a Mitotic Kinase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2000-05-09</date><risdate>2000</risdate><volume>97</volume><issue>10</issue><spage>5167</spage><epage>5172</epage><pages>5167-5172</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>hDlg, the human homologue of the Drosophila Discs-large (Dlg) tumor suppressor protein, is known to interact with the tumor suppressor protein APC and the human papillomavirus E6 transforming protein. In a two-hybrid screen, we identified a 322-aa serine/threonine kinase that binds to the PDZ2 domain of hDlg. The mRNA for this PDZ-binding kinase, or PBK, is most abundant in placenta and absent from adult brain tissue. The protein sequence of PBK has all the characteristic protein kinase subdomains and a C-terminal PDZ-binding T/SXV motif. In vitro, PBK binds specifically to PDZ2 of hDlg through its C-terminal T/SXV motif. PBK and hDlg are phosphorylated at mitosis in HeLa cells, and the mitotic phosphorylation of PBK is required for its kinase activity. In vitro, cdc2/cyclin B phosphorylates PBK. This evidence shows how PBK could link hDlg or other PDZ-containing proteins to signal transduction pathways regulating the cell cycle or cellular proliferation.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>10779557</pmid><doi>10.1073/pnas.090102397</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adaptor Proteins, Signal Transducing Adult Amino Acid Sequence Animals Antibodies APC protein Binding Sites Biochemistry Biological Sciences Brain - enzymology cdc2 protein Cell Cycle Cell Line Complementary DNA Discs Large Homolog 1 Protein Drosophila Drosophila - enzymology E6 protein Female Guanylate Kinases hDlg protein HeLa Cells Histones Humans Membrane Proteins Mice Mitogen-Activated Protein Kinase Kinases Mitosis Molecular Sequence Data Phosphatases Phosphorylation Placenta - enzymology Pregnancy Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism protein-serine/threonine kinase Proteins Proteins - chemistry Proteins - metabolism Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Spodoptera Transfection Zebrafish |
title | Characterization of PDZ-Binding Kinase, a Mitotic Kinase |
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