Interaction cloning of protein kinase C substrates
We have previously used an overlay assay technique to detect proteins that interact with protein kinase C (PKC) (Hyatt, S. L., Klauck, T., and Jaken, S. (1990) Mol. Carcinogenesis 3, 45-53). In some cases, binding proteins were also identified as substrates. Therefore, we used the overlay assay appr...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-04, Vol.268 (10), p.6858-6861 |
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| container_title | The Journal of biological chemistry |
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| creator | CHAPLINE, C RAMSAY, K KLAUCK, T JAKEN, S |
| description | We have previously used an overlay assay technique to detect proteins that interact with protein kinase C (PKC) (Hyatt, S.
L., Klauck, T., and Jaken, S. (1990) Mol. Carcinogenesis 3, 45-53). In some cases, binding proteins were also identified as
substrates. Therefore, we used the overlay assay approach to screen a rat kidney lambda gt11 cDNA library to isolate and identify
additional PKC substrates. Two clones have now been characterized. 35A is the rat homologue of the myristoylated alanine-rich
C kinase substrate (MARCKS)-related F52 cDNA, whereas 35H is a partial cDNA with substantial homology to the 3' end of beta-adducin.
Both cDNAs encode proteins that bind phosphatidyl-serine (PS) and are substrates for PKC. Phosphorylation decreased both PS
and PKC binding activities. Both proteins contain high density positive charge domains similar to that found in the major
PKC substrate MARCKS. These results demonstrate that PKC interactions with certain substrate proteins are of sufficiently
high affinity to facilitate their isolation via interaction cloning. |
| doi_str_mv | 10.1016/S0021-9258(18)53116-1 |
| format | Article |
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L., Klauck, T., and Jaken, S. (1990) Mol. Carcinogenesis 3, 45-53). In some cases, binding proteins were also identified as
substrates. Therefore, we used the overlay assay approach to screen a rat kidney lambda gt11 cDNA library to isolate and identify
additional PKC substrates. Two clones have now been characterized. 35A is the rat homologue of the myristoylated alanine-rich
C kinase substrate (MARCKS)-related F52 cDNA, whereas 35H is a partial cDNA with substantial homology to the 3' end of beta-adducin.
Both cDNAs encode proteins that bind phosphatidyl-serine (PS) and are substrates for PKC. Phosphorylation decreased both PS
and PKC binding activities. Both proteins contain high density positive charge domains similar to that found in the major
PKC substrate MARCKS. These results demonstrate that PKC interactions with certain substrate proteins are of sufficiently
high affinity to facilitate their isolation via interaction cloning.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)53116-1</identifier><identifier>PMID: 8463212</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; cDNA ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; genes ; Intracellular Signaling Peptides and Proteins ; kidney ; Membrane Proteins ; Molecular Sequence Data ; Myristoylated Alanine-Rich C Kinase Substrate ; nucleotide sequence ; predictions ; Protein Kinase C - metabolism ; Proteins - genetics ; Proteins - metabolism ; Rats ; Sequence Homology, Amino Acid ; Substrate Specificity ; Transferases</subject><ispartof>The Journal of biological chemistry, 1993-04, Vol.268 (10), p.6858-6861</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-ef2e54902f4aefaca3689defe9388d318da656031c159c9eac36e9191fac15b13</citedby><cites>FETCH-LOGICAL-c439t-ef2e54902f4aefaca3689defe9388d318da656031c159c9eac36e9191fac15b13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27931,27932</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4732595$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8463212$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CHAPLINE, C</creatorcontrib><creatorcontrib>RAMSAY, K</creatorcontrib><creatorcontrib>KLAUCK, T</creatorcontrib><creatorcontrib>JAKEN, S</creatorcontrib><title>Interaction cloning of protein kinase C substrates</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have previously used an overlay assay technique to detect proteins that interact with protein kinase C (PKC) (Hyatt, S.
L., Klauck, T., and Jaken, S. (1990) Mol. Carcinogenesis 3, 45-53). In some cases, binding proteins were also identified as
substrates. Therefore, we used the overlay assay approach to screen a rat kidney lambda gt11 cDNA library to isolate and identify
additional PKC substrates. Two clones have now been characterized. 35A is the rat homologue of the myristoylated alanine-rich
C kinase substrate (MARCKS)-related F52 cDNA, whereas 35H is a partial cDNA with substantial homology to the 3' end of beta-adducin.
Both cDNAs encode proteins that bind phosphatidyl-serine (PS) and are substrates for PKC. Phosphorylation decreased both PS
and PKC binding activities. Both proteins contain high density positive charge domains similar to that found in the major
PKC substrate MARCKS. These results demonstrate that PKC interactions with certain substrate proteins are of sufficiently
high affinity to facilitate their isolation via interaction cloning.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>cDNA</subject><subject>Cloning, Molecular</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>kidney</subject><subject>Membrane Proteins</subject><subject>Molecular Sequence Data</subject><subject>Myristoylated Alanine-Rich C Kinase Substrate</subject><subject>nucleotide sequence</subject><subject>predictions</subject><subject>Protein Kinase C - metabolism</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><subject>Transferases</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1LAzEQhoMotVZ_QmFBET2sZpJNTI5S_CgUPKjgLaTpbBvdzdZki_jv3dqlc5nDPDPz8hAyBnoDFOTtK6UMcs2EugJ1LTiAzOGADIEqnnMBH4dkuEeOyUlKn7SrQsOADFQhOQM2JGwaWozWtb4Jmaua4MMya8psHZsWfci-fLAJs0mWNvPURttiOiVHpa0SnvV9RN4fH94mz_ns5Wk6uZ_lruC6zbFkKApNWVlYLK2zXCq9wBI1V2rBQS2sFJJycCC002gdl6hBQ8eCmAMfkcvd3S7L9wZTa2qfHFaVDdhskgFZSKll0YFiB7rYpBSxNOvoaxt_DVCzdWX-XZmtCAPK_Lsy2wfj_sFmXuNiv9XL6eYX_dwmZ6sy2uB82mPFHWdCiw4732Erv1z9-Ihm7hu3wtowqbYRpBKK_wEzMHyL</recordid><startdate>19930405</startdate><enddate>19930405</enddate><creator>CHAPLINE, C</creator><creator>RAMSAY, K</creator><creator>KLAUCK, T</creator><creator>JAKEN, S</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19930405</creationdate><title>Interaction cloning of protein kinase C substrates</title><author>CHAPLINE, C ; RAMSAY, K ; KLAUCK, T ; JAKEN, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-ef2e54902f4aefaca3689defe9388d318da656031c159c9eac36e9191fac15b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>cDNA</topic><topic>Cloning, Molecular</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>kidney</topic><topic>Membrane Proteins</topic><topic>Molecular Sequence Data</topic><topic>Myristoylated Alanine-Rich C Kinase Substrate</topic><topic>nucleotide sequence</topic><topic>predictions</topic><topic>Protein Kinase C - metabolism</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CHAPLINE, C</creatorcontrib><creatorcontrib>RAMSAY, K</creatorcontrib><creatorcontrib>KLAUCK, T</creatorcontrib><creatorcontrib>JAKEN, S</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CHAPLINE, C</au><au>RAMSAY, K</au><au>KLAUCK, T</au><au>JAKEN, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction cloning of protein kinase C substrates</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-04-05</date><risdate>1993</risdate><volume>268</volume><issue>10</issue><spage>6858</spage><epage>6861</epage><pages>6858-6861</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have previously used an overlay assay technique to detect proteins that interact with protein kinase C (PKC) (Hyatt, S.
L., Klauck, T., and Jaken, S. (1990) Mol. Carcinogenesis 3, 45-53). In some cases, binding proteins were also identified as
substrates. Therefore, we used the overlay assay approach to screen a rat kidney lambda gt11 cDNA library to isolate and identify
additional PKC substrates. Two clones have now been characterized. 35A is the rat homologue of the myristoylated alanine-rich
C kinase substrate (MARCKS)-related F52 cDNA, whereas 35H is a partial cDNA with substantial homology to the 3' end of beta-adducin.
Both cDNAs encode proteins that bind phosphatidyl-serine (PS) and are substrates for PKC. Phosphorylation decreased both PS
and PKC binding activities. Both proteins contain high density positive charge domains similar to that found in the major
PKC substrate MARCKS. These results demonstrate that PKC interactions with certain substrate proteins are of sufficiently
high affinity to facilitate their isolation via interaction cloning.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8463212</pmid><doi>10.1016/S0021-9258(18)53116-1</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences cDNA Cloning, Molecular Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology genes Intracellular Signaling Peptides and Proteins kidney Membrane Proteins Molecular Sequence Data Myristoylated Alanine-Rich C Kinase Substrate nucleotide sequence predictions Protein Kinase C - metabolism Proteins - genetics Proteins - metabolism Rats Sequence Homology, Amino Acid Substrate Specificity Transferases |
| title | Interaction cloning of protein kinase C substrates |
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