MAGUIN, a Novel Neuronal Membrane-associated Guanylate Kinase-interacting Protein
Postsynaptic density (PSD)-95/Synapse-associated protein (SAP) 90 and synaptic scaffolding molecule (S-SCAM) are neuronal membrane-associated guanylate kinases. Because PSD-95/SAP90 and S-SCAM function as synaptic scaffolding proteins, identification of ligands for these proteins is important to elu...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-04, Vol.274 (17), p.11889-11896 |
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| container_title | The Journal of biological chemistry |
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| creator | Yao, I Hata, Y Ide, N Hirao, K Deguchi, M Nishioka, H Mizoguchi, A Takai, Y |
| description | Postsynaptic density (PSD)-95/Synapse-associated protein (SAP) 90 and synaptic scaffolding molecule (S-SCAM) are neuronal
membrane-associated guanylate kinases. Because PSD-95/SAP90 and S-SCAM function as synaptic scaffolding proteins, identification
of ligands for these proteins is important to elucidate the structure of synaptic junctions. Here, we report a novel protein
interacting with the PDZ domains of PSD-95/SAP90 and S-SCAM and named it MAGUIN-1 (membrane-associated guanylate kinase-interacting
protein-1). MAGUIN-1 has one sterile α motif, one PDZ, and one plekstrin homology domain. MAGUIN-1 is localized at the plasma
membrane via the plekstrin homology domain and the C-terminal region and interacts with PSD-95/SAP90 and S-SCAM via a C-terminal PDZ domain-binding motif. MAGUIN-1 has a short isoform, MAGUIN-2, which lacks a PDZ domain-binding motif. MAGUINs
are expressed in neurons and localized in the cell body and neurites and are coimmunoprecipitated with PSD-95/SAP90 and S-SCAM
from rat crude synaptosome. MAGUIN-1 may play an important role with PSD-95/SAP90 and S-SCAM to assemble the components of
synaptic junctions. |
| doi_str_mv | 10.1074/jbc.274.17.11889 |
| format | Article |
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membrane-associated guanylate kinases. Because PSD-95/SAP90 and S-SCAM function as synaptic scaffolding proteins, identification
of ligands for these proteins is important to elucidate the structure of synaptic junctions. Here, we report a novel protein
interacting with the PDZ domains of PSD-95/SAP90 and S-SCAM and named it MAGUIN-1 (membrane-associated guanylate kinase-interacting
protein-1). MAGUIN-1 has one sterile α motif, one PDZ, and one plekstrin homology domain. MAGUIN-1 is localized at the plasma
membrane via the plekstrin homology domain and the C-terminal region and interacts with PSD-95/SAP90 and S-SCAM via a C-terminal PDZ domain-binding motif. MAGUIN-1 has a short isoform, MAGUIN-2, which lacks a PDZ domain-binding motif. MAGUINs
are expressed in neurons and localized in the cell body and neurites and are coimmunoprecipitated with PSD-95/SAP90 and S-SCAM
from rat crude synaptosome. MAGUIN-1 may play an important role with PSD-95/SAP90 and S-SCAM to assemble the components of
synaptic junctions.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.17.11889</identifier><identifier>PMID: 10207009</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Membrane - metabolism ; CHO Cells ; COS Cells ; Cricetinae ; DNA, Complementary ; Guanylate Cyclase - metabolism ; Guanylate Kinases ; Molecular Sequence Data ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurons - metabolism ; Protein Binding ; Rats ; Sequence Homology, Amino Acid</subject><ispartof>The Journal of biological chemistry, 1999-04, Vol.274 (17), p.11889-11896</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c397t-e7687de4570deac3352e1c97fde3020b83c52d0a1e461c7b634f7e4fd75d13773</citedby><cites>FETCH-LOGICAL-c397t-e7687de4570deac3352e1c97fde3020b83c52d0a1e461c7b634f7e4fd75d13773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10207009$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yao, I</creatorcontrib><creatorcontrib>Hata, Y</creatorcontrib><creatorcontrib>Ide, N</creatorcontrib><creatorcontrib>Hirao, K</creatorcontrib><creatorcontrib>Deguchi, M</creatorcontrib><creatorcontrib>Nishioka, H</creatorcontrib><creatorcontrib>Mizoguchi, A</creatorcontrib><creatorcontrib>Takai, Y</creatorcontrib><title>MAGUIN, a Novel Neuronal Membrane-associated Guanylate Kinase-interacting Protein</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Postsynaptic density (PSD)-95/Synapse-associated protein (SAP) 90 and synaptic scaffolding molecule (S-SCAM) are neuronal
membrane-associated guanylate kinases. Because PSD-95/SAP90 and S-SCAM function as synaptic scaffolding proteins, identification
of ligands for these proteins is important to elucidate the structure of synaptic junctions. Here, we report a novel protein
interacting with the PDZ domains of PSD-95/SAP90 and S-SCAM and named it MAGUIN-1 (membrane-associated guanylate kinase-interacting
protein-1). MAGUIN-1 has one sterile α motif, one PDZ, and one plekstrin homology domain. MAGUIN-1 is localized at the plasma
membrane via the plekstrin homology domain and the C-terminal region and interacts with PSD-95/SAP90 and S-SCAM via a C-terminal PDZ domain-binding motif. MAGUIN-1 has a short isoform, MAGUIN-2, which lacks a PDZ domain-binding motif. MAGUINs
are expressed in neurons and localized in the cell body and neurites and are coimmunoprecipitated with PSD-95/SAP90 and S-SCAM
from rat crude synaptosome. MAGUIN-1 may play an important role with PSD-95/SAP90 and S-SCAM to assemble the components of
synaptic junctions.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>CHO Cells</subject><subject>COS Cells</subject><subject>Cricetinae</subject><subject>DNA, Complementary</subject><subject>Guanylate Cyclase - metabolism</subject><subject>Guanylate Kinases</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons - metabolism</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Sequence Homology, Amino Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EoqWwM6EMiIkUX5zEyVhVUCpoAYlKbJbjXFpX-Sh2Auq_x9AOMHEezsPzvjo9hJwDHQLl4c06U8OAh0PgQ4AkSQ9IH2jCfBbB2yHpUxqAnwZR0iMn1q6pmzCFY9IDGlBOadonL7PRZDGdX3vSmzcfWHpz7ExTy9KbYZUZWaMvrW2Uli3m3qST9bZ0X-9B19Kir-sWjVStrpfes2la1PUpOSpkafFsvwdkcXf7Or73H58m0_Ho0Vcs5a2PPE54jmHEaY5SMRYFCCrlRY7MXZclTEVBTiVgGIPiWczCgmNY5DzKgXHOBuRq17sxzXuHthWVtgrL0t3cdFbEqXtxkPwLAg8gCnnqQLoDlWmsNViIjdGVNFsBVHz7Fs63cL5dRPz4dpGLfXeXVZj_CuwEO-ByB6z0cvWpDYpMN2qF1d-eL66Lhuc</recordid><startdate>19990423</startdate><enddate>19990423</enddate><creator>Yao, I</creator><creator>Hata, Y</creator><creator>Ide, N</creator><creator>Hirao, K</creator><creator>Deguchi, M</creator><creator>Nishioka, H</creator><creator>Mizoguchi, A</creator><creator>Takai, Y</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>19990423</creationdate><title>MAGUIN, a Novel Neuronal Membrane-associated Guanylate Kinase-interacting Protein</title><author>Yao, I ; Hata, Y ; Ide, N ; Hirao, K ; Deguchi, M ; Nishioka, H ; Mizoguchi, A ; Takai, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c397t-e7687de4570deac3352e1c97fde3020b83c52d0a1e461c7b634f7e4fd75d13773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>CHO Cells</topic><topic>COS Cells</topic><topic>Cricetinae</topic><topic>DNA, Complementary</topic><topic>Guanylate Cyclase - metabolism</topic><topic>Guanylate Kinases</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons - metabolism</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yao, I</creatorcontrib><creatorcontrib>Hata, Y</creatorcontrib><creatorcontrib>Ide, N</creatorcontrib><creatorcontrib>Hirao, K</creatorcontrib><creatorcontrib>Deguchi, M</creatorcontrib><creatorcontrib>Nishioka, H</creatorcontrib><creatorcontrib>Mizoguchi, A</creatorcontrib><creatorcontrib>Takai, Y</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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>Yao, I</au><au>Hata, Y</au><au>Ide, N</au><au>Hirao, K</au><au>Deguchi, M</au><au>Nishioka, H</au><au>Mizoguchi, A</au><au>Takai, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MAGUIN, a Novel Neuronal Membrane-associated Guanylate Kinase-interacting Protein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-04-23</date><risdate>1999</risdate><volume>274</volume><issue>17</issue><spage>11889</spage><epage>11896</epage><pages>11889-11896</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Postsynaptic density (PSD)-95/Synapse-associated protein (SAP) 90 and synaptic scaffolding molecule (S-SCAM) are neuronal
membrane-associated guanylate kinases. Because PSD-95/SAP90 and S-SCAM function as synaptic scaffolding proteins, identification
of ligands for these proteins is important to elucidate the structure of synaptic junctions. Here, we report a novel protein
interacting with the PDZ domains of PSD-95/SAP90 and S-SCAM and named it MAGUIN-1 (membrane-associated guanylate kinase-interacting
protein-1). MAGUIN-1 has one sterile α motif, one PDZ, and one plekstrin homology domain. MAGUIN-1 is localized at the plasma
membrane via the plekstrin homology domain and the C-terminal region and interacts with PSD-95/SAP90 and S-SCAM via a C-terminal PDZ domain-binding motif. MAGUIN-1 has a short isoform, MAGUIN-2, which lacks a PDZ domain-binding motif. MAGUINs
are expressed in neurons and localized in the cell body and neurites and are coimmunoprecipitated with PSD-95/SAP90 and S-SCAM
from rat crude synaptosome. MAGUIN-1 may play an important role with PSD-95/SAP90 and S-SCAM to assemble the components of
synaptic junctions.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>10207009</pmid><doi>10.1074/jbc.274.17.11889</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cell Membrane - metabolism CHO Cells COS Cells Cricetinae DNA, Complementary Guanylate Cyclase - metabolism Guanylate Kinases Molecular Sequence Data Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurons - metabolism Protein Binding Rats Sequence Homology, Amino Acid |
| title | MAGUIN, a Novel Neuronal Membrane-associated Guanylate Kinase-interacting Protein |
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