The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle
Phosphorylase kinase is a key enzyme in regulating glycogenolytic flux in skeletal muscle in response to changing energy demands. In the present study, we sought to identify interacting proteins of phosphorylase kinase by yeast two-hybrid screening. Screening a rabbit skeletal muscle cDNA library wi...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-07, Vol.345 (4), p.1592-1599 |
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| creator | Archila, Soleil King, Mark A. Carlson, Gerald M. Rice, Nancy A. |
| description | Phosphorylase kinase is a key enzyme in regulating glycogenolytic flux in skeletal muscle in response to changing energy demands. In the present study, we sought to identify interacting proteins of phosphorylase kinase by yeast two-hybrid screening. Screening a rabbit skeletal muscle cDNA library with the exposed C-terminus of the α subunit (residues 1060–1237), we identified eight independent, yet overlapping, constructs of cdc42-interacting protein 4 (CIP4). Immunocytochemistry indicated that CIP4 colocalized with phosphorylase kinase in vivo, and the cognate binding domain on CIP4 was determined to lie between residues 398 and 545. While this region of CIP4 does contain a known src homology 3 domain, transient transfections and coimmunoprecipitation experiments showed that this domain is not responsible for the dimeric interaction. Based upon sequence analysis the association is inferred to be mediated by two proline-rich sequences in CIP4, residues 436–439 and 441–444, that bind to a cognate WW domain found between residues 1107 and 1129 of PhKα. |
| doi_str_mv | 10.1016/j.bbrc.2006.05.073 |
| format | Article |
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In the present study, we sought to identify interacting proteins of phosphorylase kinase by yeast two-hybrid screening. Screening a rabbit skeletal muscle cDNA library with the exposed C-terminus of the α subunit (residues 1060–1237), we identified eight independent, yet overlapping, constructs of cdc42-interacting protein 4 (CIP4). Immunocytochemistry indicated that CIP4 colocalized with phosphorylase kinase in vivo, and the cognate binding domain on CIP4 was determined to lie between residues 398 and 545. While this region of CIP4 does contain a known src homology 3 domain, transient transfections and coimmunoprecipitation experiments showed that this domain is not responsible for the dimeric interaction. 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In the present study, we sought to identify interacting proteins of phosphorylase kinase by yeast two-hybrid screening. Screening a rabbit skeletal muscle cDNA library with the exposed C-terminus of the α subunit (residues 1060–1237), we identified eight independent, yet overlapping, constructs of cdc42-interacting protein 4 (CIP4). Immunocytochemistry indicated that CIP4 colocalized with phosphorylase kinase in vivo, and the cognate binding domain on CIP4 was determined to lie between residues 398 and 545. While this region of CIP4 does contain a known src homology 3 domain, transient transfections and coimmunoprecipitation experiments showed that this domain is not responsible for the dimeric interaction. Based upon sequence analysis the association is inferred to be mediated by two proline-rich sequences in CIP4, residues 436–439 and 441–444, that bind to a cognate WW domain found between residues 1107 and 1129 of PhKα.</description><subject>Actin</subject><subject>Animals</subject><subject>beta-Galactosidase - metabolism</subject><subject>Blotting, Western</subject><subject>Cdc-42-interacting protein</subject><subject>Cell Line</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Lac Operon - genetics</subject><subject>Mice</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Minor Histocompatibility Antigens</subject><subject>Muscle, Skeletal - cytology</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Phosphorylase kinase</subject><subject>Phosphorylase Kinase - genetics</subject><subject>Phosphorylase Kinase - metabolism</subject><subject>Plasmids - genetics</subject><subject>Protein Binding</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>Rabbits</subject><subject>src Homology Domains - genetics</subject><subject>Two-hybrid</subject><subject>Two-Hybrid System Techniques</subject><subject>WW domain</subject><subject>Yeasts - genetics</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1PwzAMhiMEYuPjD3BAPXFrsds0bSUuaOJLQuIyJG5Rmnpbtq4dSQYav55Mm4ATB8sHP35lP4xdICQIKK7nSV1bnaQAIoE8gSI7YEOECuIUgR-yIYRJnFb4NmAnzs0BELmojtkARZHlkPIh-xzPKNIb37sFteRVG_V2qjrzZbpptLK9J9NFo0bzNDadJ6u0_zvhkXKu10Z5ctGn8bNoNetdKLtplaNoYbptC-RP_nLtdEtn7GiiWkfn-37KXu_vxqPH-Pnl4Wl0-xzrLOc-FnVRNhko4FwApjrPaoFNoQoUdVPmyHWhSt0IjlzVqMsSqipX2aTI0jx8WGen7GqXGy5-X5PzcmmcprZVHfVrJ0UJAqDCAKY7UNveOUsTubJmqexGIsitbjmXW91yq1tCLoPusHS5T1_XS2p-V_Z-A3CzAyj8-GHISqcNdZoaY0l72fTmv_xvXa-SZw</recordid><startdate>20060714</startdate><enddate>20060714</enddate><creator>Archila, Soleil</creator><creator>King, Mark A.</creator><creator>Carlson, Gerald M.</creator><creator>Rice, Nancy A.</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20060714</creationdate><title>The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle</title><author>Archila, Soleil ; King, Mark A. ; Carlson, Gerald M. ; Rice, Nancy A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-6b78d30a0446012c53b61d7a716bd8514c7a8cd6414ab1c880995a3f7325350b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Actin</topic><topic>Animals</topic><topic>beta-Galactosidase - metabolism</topic><topic>Blotting, Western</topic><topic>Cdc-42-interacting protein</topic><topic>Cell Line</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Lac Operon - genetics</topic><topic>Mice</topic><topic>Microtubule-Associated Proteins - genetics</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Minor Histocompatibility Antigens</topic><topic>Muscle, Skeletal - cytology</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Phosphorylase kinase</topic><topic>Phosphorylase Kinase - genetics</topic><topic>Phosphorylase Kinase - metabolism</topic><topic>Plasmids - genetics</topic><topic>Protein Binding</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>Rabbits</topic><topic>src Homology Domains - genetics</topic><topic>Two-hybrid</topic><topic>Two-Hybrid System Techniques</topic><topic>WW domain</topic><topic>Yeasts - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Archila, Soleil</creatorcontrib><creatorcontrib>King, Mark A.</creatorcontrib><creatorcontrib>Carlson, Gerald M.</creatorcontrib><creatorcontrib>Rice, Nancy 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>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Archila, Soleil</au><au>King, Mark A.</au><au>Carlson, Gerald M.</au><au>Rice, Nancy A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-07-14</date><risdate>2006</risdate><volume>345</volume><issue>4</issue><spage>1592</spage><epage>1599</epage><pages>1592-1599</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Phosphorylase kinase is a key enzyme in regulating glycogenolytic flux in skeletal muscle in response to changing energy demands. In the present study, we sought to identify interacting proteins of phosphorylase kinase by yeast two-hybrid screening. Screening a rabbit skeletal muscle cDNA library with the exposed C-terminus of the α subunit (residues 1060–1237), we identified eight independent, yet overlapping, constructs of cdc42-interacting protein 4 (CIP4). Immunocytochemistry indicated that CIP4 colocalized with phosphorylase kinase in vivo, and the cognate binding domain on CIP4 was determined to lie between residues 398 and 545. While this region of CIP4 does contain a known src homology 3 domain, transient transfections and coimmunoprecipitation experiments showed that this domain is not responsible for the dimeric interaction. 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| subjects | Actin Animals beta-Galactosidase - metabolism Blotting, Western Cdc-42-interacting protein Cell Line Humans Immunoprecipitation Lac Operon - genetics Mice Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Minor Histocompatibility Antigens Muscle, Skeletal - cytology Muscle, Skeletal - metabolism Phosphorylase kinase Phosphorylase Kinase - genetics Phosphorylase Kinase - metabolism Plasmids - genetics Protein Binding Protein Subunits - genetics Protein Subunits - metabolism Rabbits src Homology Domains - genetics Two-hybrid Two-Hybrid System Techniques WW domain Yeasts - genetics |
| title | The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle |
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