Analysis of the Role of Calmodulin Binding and Sequestration in Neuromodulin (GAP-43) Function
We demonstrated previously that forced expression of the neuronal phosphoprotein neuromodulin (also known as GAP-43, F1, B-50, and p57) in mouse anterior pituitary AtT-20 cells enhances depolarization-mediated secretion and alters cellular morphology. Here we analyze the role of calmodulin binding b...
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| Veröffentlicht in: | The Journal of biological chemistry 1996-10, Vol.271 (43), p.26698-26705 |
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| container_issue | 43 |
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| container_title | The Journal of biological chemistry |
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| creator | Gamby, C Waage, M C Allen, R G Baizer, L |
| description | We demonstrated previously that forced expression of the neuronal phosphoprotein neuromodulin (also known as GAP-43, F1, B-50,
and p57) in mouse anterior pituitary AtT-20 cells enhances depolarization-mediated secretion and alters cellular morphology.
Here we analyze the role of calmodulin binding by neuromodulin in these responses. In cells expressing wild-type neuromodulin,
a complex with calmodulin that is sensitive to intracellular calcium and phosphorylation is localized to the plasma membrane.
Transfection of several mutant forms of neuromodulin shows that the effects of this protein on secretion are dependent on
both calmodulin binding and association with the plasma membrane. In contrast, the morphological changes depend only on membrane
association. Thus, the multitude of effects of neuromodulin noted in previous studies may result from divergent properties
of this protein. |
| doi_str_mv | 10.1074/jbc.271.43.26698 |
| format | Article |
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and p57) in mouse anterior pituitary AtT-20 cells enhances depolarization-mediated secretion and alters cellular morphology.
Here we analyze the role of calmodulin binding by neuromodulin in these responses. In cells expressing wild-type neuromodulin,
a complex with calmodulin that is sensitive to intracellular calcium and phosphorylation is localized to the plasma membrane.
Transfection of several mutant forms of neuromodulin shows that the effects of this protein on secretion are dependent on
both calmodulin binding and association with the plasma membrane. In contrast, the morphological changes depend only on membrane
association. Thus, the multitude of effects of neuromodulin noted in previous studies may result from divergent properties
of this protein.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.271.43.26698</identifier><identifier>PMID: 8900147</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Calcium - metabolism ; Calmodulin - metabolism ; Calmodulin-Binding Proteins - genetics ; Calmodulin-Binding Proteins - metabolism ; Cell Line ; Cross-Linking Reagents ; GAP-43 Protein ; Hippocampus - cytology ; Hippocampus - metabolism ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Mice ; Mutation ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurons - cytology ; Neurons - metabolism ; Phosphorylation ; Potassium - metabolism ; Protein Kinase C - metabolism</subject><ispartof>The Journal of biological chemistry, 1996-10, Vol.271 (43), p.26698-26705</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-956a35518a5ce1facdbf88979fc156354d43486be7c1454bd5e6a4a8bc22d2883</citedby><cites>FETCH-LOGICAL-c462t-956a35518a5ce1facdbf88979fc156354d43486be7c1454bd5e6a4a8bc22d2883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8900147$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gamby, C</creatorcontrib><creatorcontrib>Waage, M C</creatorcontrib><creatorcontrib>Allen, R G</creatorcontrib><creatorcontrib>Baizer, L</creatorcontrib><title>Analysis of the Role of Calmodulin Binding and Sequestration in Neuromodulin (GAP-43) Function</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We demonstrated previously that forced expression of the neuronal phosphoprotein neuromodulin (also known as GAP-43, F1, B-50,
and p57) in mouse anterior pituitary AtT-20 cells enhances depolarization-mediated secretion and alters cellular morphology.
Here we analyze the role of calmodulin binding by neuromodulin in these responses. In cells expressing wild-type neuromodulin,
a complex with calmodulin that is sensitive to intracellular calcium and phosphorylation is localized to the plasma membrane.
Transfection of several mutant forms of neuromodulin shows that the effects of this protein on secretion are dependent on
both calmodulin binding and association with the plasma membrane. In contrast, the morphological changes depend only on membrane
association. Thus, the multitude of effects of neuromodulin noted in previous studies may result from divergent properties
of this protein.</description><subject>Animals</subject><subject>Calcium - metabolism</subject><subject>Calmodulin - metabolism</subject><subject>Calmodulin-Binding Proteins - genetics</subject><subject>Calmodulin-Binding Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cross-Linking Reagents</subject><subject>GAP-43 Protein</subject><subject>Hippocampus - cytology</subject><subject>Hippocampus - metabolism</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mice</subject><subject>Mutation</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons - cytology</subject><subject>Neurons - metabolism</subject><subject>Phosphorylation</subject><subject>Potassium - metabolism</subject><subject>Protein Kinase C - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1LwzAYh4Moc07vXoQeRPTQms82Pc7hpjBU_ABPhjRNt4y2mUmL7L-3-1Dw5HvJC7_n_REeAE4RjBBM6PUiUxFOUERJhOM45XugjyAnIWHofR_0IcQoTDHjh-DI-wXshqaoB3o8hRDRpA8-hrUsV974wBZBM9fBsy31eh_JsrJ5W5o6uDF1bupZIOs8eNGfrfaNk42xddCFD7p19oe8nAyfQkqugnFbqzVxDA4KWXp9snsH4G18-zq6C6ePk_vRcBoqGuMmTFksCWOIS6Y0KqTKs4LzNEkLhVhMGM0poTzOdKIQZTTLmY4llTxTGOeYczIAF9vepbObD4rKeKXLUtbatl4knGEMY_wviFiS0BSSDoRbUDnrvdOFWDpTSbcSCIq1e9G5F517QYnYuO9OznbdbVbp_PdgJ7vLz7f53MzmX8ZpkRmr5rr6W_MNJ7iKjw</recordid><startdate>19961025</startdate><enddate>19961025</enddate><creator>Gamby, C</creator><creator>Waage, M C</creator><creator>Allen, R G</creator><creator>Baizer, L</creator><general>American Society for Biochemistry and Molecular Biology</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>7QP</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>19961025</creationdate><title>Analysis of the Role of Calmodulin Binding and Sequestration in Neuromodulin (GAP-43) Function</title><author>Gamby, C ; Waage, M C ; Allen, R G ; Baizer, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-956a35518a5ce1facdbf88979fc156354d43486be7c1454bd5e6a4a8bc22d2883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>Calcium - metabolism</topic><topic>Calmodulin - metabolism</topic><topic>Calmodulin-Binding Proteins - genetics</topic><topic>Calmodulin-Binding Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cross-Linking Reagents</topic><topic>GAP-43 Protein</topic><topic>Hippocampus - cytology</topic><topic>Hippocampus - metabolism</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Mice</topic><topic>Mutation</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons - cytology</topic><topic>Neurons - metabolism</topic><topic>Phosphorylation</topic><topic>Potassium - metabolism</topic><topic>Protein Kinase C - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gamby, C</creatorcontrib><creatorcontrib>Waage, M C</creatorcontrib><creatorcontrib>Allen, R G</creatorcontrib><creatorcontrib>Baizer, L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences 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>Gamby, C</au><au>Waage, M C</au><au>Allen, R G</au><au>Baizer, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the Role of Calmodulin Binding and Sequestration in Neuromodulin (GAP-43) Function</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-10-25</date><risdate>1996</risdate><volume>271</volume><issue>43</issue><spage>26698</spage><epage>26705</epage><pages>26698-26705</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>We demonstrated previously that forced expression of the neuronal phosphoprotein neuromodulin (also known as GAP-43, F1, B-50,
and p57) in mouse anterior pituitary AtT-20 cells enhances depolarization-mediated secretion and alters cellular morphology.
Here we analyze the role of calmodulin binding by neuromodulin in these responses. In cells expressing wild-type neuromodulin,
a complex with calmodulin that is sensitive to intracellular calcium and phosphorylation is localized to the plasma membrane.
Transfection of several mutant forms of neuromodulin shows that the effects of this protein on secretion are dependent on
both calmodulin binding and association with the plasma membrane. In contrast, the morphological changes depend only on membrane
association. Thus, the multitude of effects of neuromodulin noted in previous studies may result from divergent properties
of this protein.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8900147</pmid><doi>10.1074/jbc.271.43.26698</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1996-10, Vol.271 (43), p.26698-26705 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78522062 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Calcium - metabolism Calmodulin - metabolism Calmodulin-Binding Proteins - genetics Calmodulin-Binding Proteins - metabolism Cell Line Cross-Linking Reagents GAP-43 Protein Hippocampus - cytology Hippocampus - metabolism Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Mice Mutation Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurons - cytology Neurons - metabolism Phosphorylation Potassium - metabolism Protein Kinase C - metabolism |
| title | Analysis of the Role of Calmodulin Binding and Sequestration in Neuromodulin (GAP-43) Function |
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