Cloning and characterization of AKAP 95, a nuclear protein that associates with the regulatory subunit of type II cAMP-dependent protein kinase
The subcellular location of the type II cAMP-dependent protein kinase is dictated by the interaction of the regulatory subunit (RII) with A-kinase anchor proteins (AKAPs). Using an interaction cloning strategy with RII alpha as a probe, we have isolated cDNAs encoding a novel 761-amino acid protein...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-03, Vol.269 (10), p.7658-7665 |
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| container_issue | 10 |
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| container_title | The Journal of biological chemistry |
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| creator | COGHLAN, V. M LANGEBERG, L. K FERNANDEZ, A LAMB, N. J. C SCOTT, J. D |
| description | The subcellular location of the type II cAMP-dependent protein kinase is dictated by the interaction of the regulatory subunit
(RII) with A-kinase anchor proteins (AKAPs). Using an interaction cloning strategy with RII alpha as a probe, we have isolated
cDNAs encoding a novel 761-amino acid protein (named AKAP 95) that contains both RII- and DNA-binding domains. Deletion analysis
and peptide studies revealed that the RII-binding domain of AKAP 95 is located between residues 642 and 659 and includes a
predicted amphipathic helix. Zinc overlay and DNA binding studies suggest that the DNA-binding domain is composed of two CC/HH-type
zinc fingers between residues 464 and 486 and residues 553 and 576. The AKAP was detected in a nuclear matrix fraction, and
immunofluorescence using purified anti-AKAP 95 antibodies revealed a distinct nuclear staining in a variety of cell types.
Direct overlay of fluorescein isothiocyanate-labeled RII alpha onto fixed rat embryo fibroblasts showed that high-affinity
binding sites for RII exist in the nucleus and that these sites are blocked by an anchoring inhibitor peptide. Furthermore,
AKAP 95 was detected in preparations of RII that were purified from cellular extracts using cAMP-agarose. The results suggest
that AKAP 95 could play a role in targeting type II cAMP-dependent protein kinase for cAMP-responsive nuclear events. |
| doi_str_mv | 10.1016/S0021-9258(17)37338-6 |
| format | Article |
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(RII) with A-kinase anchor proteins (AKAPs). Using an interaction cloning strategy with RII alpha as a probe, we have isolated
cDNAs encoding a novel 761-amino acid protein (named AKAP 95) that contains both RII- and DNA-binding domains. Deletion analysis
and peptide studies revealed that the RII-binding domain of AKAP 95 is located between residues 642 and 659 and includes a
predicted amphipathic helix. Zinc overlay and DNA binding studies suggest that the DNA-binding domain is composed of two CC/HH-type
zinc fingers between residues 464 and 486 and residues 553 and 576. The AKAP was detected in a nuclear matrix fraction, and
immunofluorescence using purified anti-AKAP 95 antibodies revealed a distinct nuclear staining in a variety of cell types.
Direct overlay of fluorescein isothiocyanate-labeled RII alpha onto fixed rat embryo fibroblasts showed that high-affinity
binding sites for RII exist in the nucleus and that these sites are blocked by an anchoring inhibitor peptide. Furthermore,
AKAP 95 was detected in preparations of RII that were purified from cellular extracts using cAMP-agarose. The results suggest
that AKAP 95 could play a role in targeting type II cAMP-dependent protein kinase for cAMP-responsive nuclear events.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)37338-6</identifier><identifier>PMID: 8125992</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>A Kinase Anchor Proteins ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Base Sequence ; Binding and carrier proteins ; Biological and medical sciences ; Chromatography, Gel ; Cloning, Molecular ; Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit ; Cyclic AMP-Dependent Protein Kinase Type II ; Cyclic AMP-Dependent Protein Kinases - metabolism ; DNA, Complementary ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - isolation & purification ; DNA-Binding Proteins - metabolism ; Electrophoresis, Polyacrylamide Gel ; Fluorescent Antibody Technique ; Fundamental and applied biological sciences. Psychology ; Molecular Sequence Data ; Nuclear Proteins - genetics ; Nuclear Proteins - isolation & purification ; Nuclear Proteins - metabolism ; Protein Binding ; Proteins ; Rats ; Subcellular Fractions - metabolism ; Zinc Fingers</subject><ispartof>The Journal of biological chemistry, 1994-03, Vol.269 (10), p.7658-7665</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-ab8d5543068a0104f828ab9e6d4c046dada16a02e0088b35bd63523969e801703</citedby><cites>FETCH-LOGICAL-c439t-ab8d5543068a0104f828ab9e6d4c046dada16a02e0088b35bd63523969e801703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4015238$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8125992$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>COGHLAN, V. M</creatorcontrib><creatorcontrib>LANGEBERG, L. K</creatorcontrib><creatorcontrib>FERNANDEZ, A</creatorcontrib><creatorcontrib>LAMB, N. J. C</creatorcontrib><creatorcontrib>SCOTT, J. D</creatorcontrib><title>Cloning and characterization of AKAP 95, a nuclear protein that associates with the regulatory subunit of type II cAMP-dependent protein kinase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The subcellular location of the type II cAMP-dependent protein kinase is dictated by the interaction of the regulatory subunit
(RII) with A-kinase anchor proteins (AKAPs). Using an interaction cloning strategy with RII alpha as a probe, we have isolated
cDNAs encoding a novel 761-amino acid protein (named AKAP 95) that contains both RII- and DNA-binding domains. Deletion analysis
and peptide studies revealed that the RII-binding domain of AKAP 95 is located between residues 642 and 659 and includes a
predicted amphipathic helix. Zinc overlay and DNA binding studies suggest that the DNA-binding domain is composed of two CC/HH-type
zinc fingers between residues 464 and 486 and residues 553 and 576. The AKAP was detected in a nuclear matrix fraction, and
immunofluorescence using purified anti-AKAP 95 antibodies revealed a distinct nuclear staining in a variety of cell types.
Direct overlay of fluorescein isothiocyanate-labeled RII alpha onto fixed rat embryo fibroblasts showed that high-affinity
binding sites for RII exist in the nucleus and that these sites are blocked by an anchoring inhibitor peptide. Furthermore,
AKAP 95 was detected in preparations of RII that were purified from cellular extracts using cAMP-agarose. The results suggest
that AKAP 95 could play a role in targeting type II cAMP-dependent protein kinase for cAMP-responsive nuclear events.</description><subject>A Kinase Anchor Proteins</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Gel</subject><subject>Cloning, Molecular</subject><subject>Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit</subject><subject>Cyclic AMP-Dependent Protein Kinase Type II</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>DNA, Complementary</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - isolation & purification</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Molecular Sequence Data</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - isolation & purification</subject><subject>Nuclear Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Rats</subject><subject>Subcellular Fractions - metabolism</subject><subject>Zinc Fingers</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkd-K1DAUh4Mo67j6CAsBRRSsJk2TJpfD4J_BFRdU8C6cpqfTaCedTVKW8SV8ZTs7w9yam0DOd37nhI-QK87ecsbVu2-MlbwwpdSveP1a1ELoQj0gC860KITkPx-SxRl5TJ6k9IvNpzL8glxoXkpjygX5uxrG4MOGQmip6yGCyxj9H8h-DHTs6PLz8oYa-YYCDZMbECLdxTGjDzT3kCmkNDoPGRO987mfH5FG3EwD5DHuaZqaKfh8SMr7HdL1mrrll5uixR2GFkM-p_32ARI-JY86GBI-O92X5MeH999Xn4rrrx_Xq-V14SphcgGNbqWsBFMaGGdVp0sNjUHVVo5VqoUWuAJWImNaN0I2rRKyFEYZ1IzXTFySl8fcefzthCnbrU8OhwECjlOytRJaa8X_C3KlmeJlOYPyCLo4phSxs7votxD3ljN7MGbvjdmDDstre2_Mqrnv6jRgarbYnrtOiub6i1MdkoOhixCcT2esYnz-mJ6x50es95v-zke0jR9dj1tbKnNYoVZSi38S6anY</recordid><startdate>19940311</startdate><enddate>19940311</enddate><creator>COGHLAN, V. M</creator><creator>LANGEBERG, L. K</creator><creator>FERNANDEZ, A</creator><creator>LAMB, N. J. C</creator><creator>SCOTT, J. D</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19940311</creationdate><title>Cloning and characterization of AKAP 95, a nuclear protein that associates with the regulatory subunit of type II cAMP-dependent protein kinase</title><author>COGHLAN, V. M ; LANGEBERG, L. K ; FERNANDEZ, A ; LAMB, N. J. C ; SCOTT, J. D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-ab8d5543068a0104f828ab9e6d4c046dada16a02e0088b35bd63523969e801703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>A Kinase Anchor Proteins</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Gel</topic><topic>Cloning, Molecular</topic><topic>Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit</topic><topic>Cyclic AMP-Dependent Protein Kinase Type II</topic><topic>Cyclic AMP-Dependent Protein Kinases - metabolism</topic><topic>DNA, Complementary</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - isolation & purification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fluorescent Antibody Technique</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Molecular Sequence Data</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - isolation & purification</topic><topic>Nuclear Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Rats</topic><topic>Subcellular Fractions - metabolism</topic><topic>Zinc Fingers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>COGHLAN, V. M</creatorcontrib><creatorcontrib>LANGEBERG, L. K</creatorcontrib><creatorcontrib>FERNANDEZ, A</creatorcontrib><creatorcontrib>LAMB, N. J. C</creatorcontrib><creatorcontrib>SCOTT, J. D</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>Nucleic Acids Abstracts</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>COGHLAN, V. M</au><au>LANGEBERG, L. K</au><au>FERNANDEZ, A</au><au>LAMB, N. J. C</au><au>SCOTT, J. D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and characterization of AKAP 95, a nuclear protein that associates with the regulatory subunit of type II cAMP-dependent protein kinase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-03-11</date><risdate>1994</risdate><volume>269</volume><issue>10</issue><spage>7658</spage><epage>7665</epage><pages>7658-7665</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The subcellular location of the type II cAMP-dependent protein kinase is dictated by the interaction of the regulatory subunit
(RII) with A-kinase anchor proteins (AKAPs). Using an interaction cloning strategy with RII alpha as a probe, we have isolated
cDNAs encoding a novel 761-amino acid protein (named AKAP 95) that contains both RII- and DNA-binding domains. Deletion analysis
and peptide studies revealed that the RII-binding domain of AKAP 95 is located between residues 642 and 659 and includes a
predicted amphipathic helix. Zinc overlay and DNA binding studies suggest that the DNA-binding domain is composed of two CC/HH-type
zinc fingers between residues 464 and 486 and residues 553 and 576. The AKAP was detected in a nuclear matrix fraction, and
immunofluorescence using purified anti-AKAP 95 antibodies revealed a distinct nuclear staining in a variety of cell types.
Direct overlay of fluorescein isothiocyanate-labeled RII alpha onto fixed rat embryo fibroblasts showed that high-affinity
binding sites for RII exist in the nucleus and that these sites are blocked by an anchoring inhibitor peptide. Furthermore,
AKAP 95 was detected in preparations of RII that were purified from cellular extracts using cAMP-agarose. The results suggest
that AKAP 95 could play a role in targeting type II cAMP-dependent protein kinase for cAMP-responsive nuclear events.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8125992</pmid><doi>10.1016/S0021-9258(17)37338-6</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1994-03, Vol.269 (10), p.7658-7665 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76388861 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | A Kinase Anchor Proteins Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Binding and carrier proteins Biological and medical sciences Chromatography, Gel Cloning, Molecular Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit Cyclic AMP-Dependent Protein Kinase Type II Cyclic AMP-Dependent Protein Kinases - metabolism DNA, Complementary DNA-Binding Proteins - genetics DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Molecular Sequence Data Nuclear Proteins - genetics Nuclear Proteins - isolation & purification Nuclear Proteins - metabolism Protein Binding Proteins Rats Subcellular Fractions - metabolism Zinc Fingers |
| title | Cloning and characterization of AKAP 95, a nuclear protein that associates with the regulatory subunit of type II cAMP-dependent protein kinase |
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