Synaptic adhesion molecules in Cadm family at the neuromuscular junction
RA175/SynCAM1/Cadm1 (Cadm1), a member of the immunoglobulin superfamily, is a synaptic cell adhesion molecule that has a PDZ‐binding motif at the C‐terminal region. It promotes the formation of presynaptic terminals and induces functional synapses in the central nervous system. Cadm1‐deficient (knoc...
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| Veröffentlicht in: | Cell biology international 2013-07, Vol.37 (7), p.731-736 |
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| creator | Tanabe, Yuko Fujita, Eriko Hayashi, Yukiko K. Zhu, Xinran Lubbert, Hermann Mezaki, Yoshihiro Senoo, Haruki Momoi, Takashi |
| description | RA175/SynCAM1/Cadm1 (Cadm1), a member of the immunoglobulin superfamily, is a synaptic cell adhesion molecule that has a PDZ‐binding motif at the C‐terminal region. It promotes the formation of presynaptic terminals and induces functional synapses in the central nervous system. Cadm1‐deficient (knockout [KO]) mice show behavioral abnormalities, including excessive aggression and anxiety, but do not show any symptoms of neuromuscular disorder, although neuromuscular junctions (NMJs) have structures similar to synapses. We have examined the expression of members of the Cadm family in the mouse muscle tissues. Cadm4 and Cadm1 were major components of the Cadm family, and Cadm3 was faintly detected, but Cadm2 was not detected by RT‐PCR. Cadm4 as well as Cadm1 colocalized with alpha‐bungarotoxin at the NMJs and interacted with the multiple PDZ domain protein Mupp1. Cadm4 was expressed in Cadm1‐KO mice and might compensate for Cadm1 loss through interactions with Mupp1. |
| doi_str_mv | 10.1002/cbin.10092 |
| format | Article |
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It promotes the formation of presynaptic terminals and induces functional synapses in the central nervous system. Cadm1‐deficient (knockout [KO]) mice show behavioral abnormalities, including excessive aggression and anxiety, but do not show any symptoms of neuromuscular disorder, although neuromuscular junctions (NMJs) have structures similar to synapses. We have examined the expression of members of the Cadm family in the mouse muscle tissues. Cadm4 and Cadm1 were major components of the Cadm family, and Cadm3 was faintly detected, but Cadm2 was not detected by RT‐PCR. Cadm4 as well as Cadm1 colocalized with alpha‐bungarotoxin at the NMJs and interacted with the multiple PDZ domain protein Mupp1. Cadm4 was expressed in Cadm1‐KO mice and might compensate for Cadm1 loss through interactions with Mupp1.</description><identifier>ISSN: 1065-6995</identifier><identifier>EISSN: 1095-8355</identifier><identifier>DOI: 10.1002/cbin.10092</identifier><identifier>PMID: 23505055</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Animals ; Bungarotoxins - metabolism ; Cadm1 ; Cadm4 ; Carrier Proteins - metabolism ; Cell Adhesion Molecule-1 ; Cell Adhesion Molecules - chemistry ; Cell Adhesion Molecules - genetics ; Cell Adhesion Molecules - metabolism ; Immunoglobulins - chemistry ; Immunoglobulins - genetics ; Immunoglobulins - metabolism ; Immunohistochemistry ; Mice ; Mice, Knockout ; Mupp1 ; Muscle, Skeletal - metabolism ; neuromuscular junction ; Neuromuscular Junction - metabolism ; PDZ ; PDZ Domains ; Protein Binding ; Recombinant Fusion Proteins - analysis ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism</subject><ispartof>Cell biology international, 2013-07, Vol.37 (7), p.731-736</ispartof><rights>2013 International Federation for Cell Biology</rights><rights>2013 International Federation for Cell Biology.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5032-d241d6cc263f994dbdde2e2f05985d364dd1177d1f3c0e48976c265dc77f8e7f3</citedby><cites>FETCH-LOGICAL-c5032-d241d6cc263f994dbdde2e2f05985d364dd1177d1f3c0e48976c265dc77f8e7f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcbin.10092$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcbin.10092$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23505055$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tanabe, Yuko</creatorcontrib><creatorcontrib>Fujita, Eriko</creatorcontrib><creatorcontrib>Hayashi, Yukiko K.</creatorcontrib><creatorcontrib>Zhu, Xinran</creatorcontrib><creatorcontrib>Lubbert, Hermann</creatorcontrib><creatorcontrib>Mezaki, Yoshihiro</creatorcontrib><creatorcontrib>Senoo, Haruki</creatorcontrib><creatorcontrib>Momoi, Takashi</creatorcontrib><title>Synaptic adhesion molecules in Cadm family at the neuromuscular junction</title><title>Cell biology international</title><addtitle>Cell Biol Int</addtitle><description>RA175/SynCAM1/Cadm1 (Cadm1), a member of the immunoglobulin superfamily, is a synaptic cell adhesion molecule that has a PDZ‐binding motif at the C‐terminal region. It promotes the formation of presynaptic terminals and induces functional synapses in the central nervous system. Cadm1‐deficient (knockout [KO]) mice show behavioral abnormalities, including excessive aggression and anxiety, but do not show any symptoms of neuromuscular disorder, although neuromuscular junctions (NMJs) have structures similar to synapses. We have examined the expression of members of the Cadm family in the mouse muscle tissues. Cadm4 and Cadm1 were major components of the Cadm family, and Cadm3 was faintly detected, but Cadm2 was not detected by RT‐PCR. Cadm4 as well as Cadm1 colocalized with alpha‐bungarotoxin at the NMJs and interacted with the multiple PDZ domain protein Mupp1. Cadm4 was expressed in Cadm1‐KO mice and might compensate for Cadm1 loss through interactions with Mupp1.</description><subject>Animals</subject><subject>Bungarotoxins - metabolism</subject><subject>Cadm1</subject><subject>Cadm4</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Adhesion Molecule-1</subject><subject>Cell Adhesion Molecules - chemistry</subject><subject>Cell Adhesion Molecules - genetics</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Immunoglobulins - chemistry</subject><subject>Immunoglobulins - genetics</subject><subject>Immunoglobulins - metabolism</subject><subject>Immunohistochemistry</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mupp1</subject><subject>Muscle, Skeletal - metabolism</subject><subject>neuromuscular junction</subject><subject>Neuromuscular Junction - metabolism</subject><subject>PDZ</subject><subject>PDZ Domains</subject><subject>Protein Binding</subject><subject>Recombinant Fusion Proteins - analysis</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><issn>1065-6995</issn><issn>1095-8355</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS0EolDY8AHIS4QUsOPYjpe0QKmoQOIhlpZrT4RLHiVOBP17EgIs0SxmFudeaQ5CR5ScUULic7v0ZX-peAvtUaJ4lDLOt_tb8EgoxUdoP4QVIZQmqdhFo5hx0g3fQzePm9KsG2-xca8QfFXiosrBtjkE7Es8Na7AmSl8vsGmwc0r4BLauira0DGmxqu2tE0XO0A7mckDHP7sMXq-vnqa3kSL-9l8erGILCcsjlycUCesjQXLlErc0jmIIc4IVyl3TCTOUSqloxmzBJJUSdGx3FkpsxRkxsboZOhd19V7C6HRhQ8W8tyUULVBUya6zyiTSYeeDqitqxBqyPS69oWpN5oS3ZvTvTn9ba6Dj39622UB7g_9VdUBdAA-fA6bf6r0dDK_-y2NhowPDXz-ZUz9poVkkuuXu5lObh8mKr2c6Ef2BZZwh7c</recordid><startdate>201307</startdate><enddate>201307</enddate><creator>Tanabe, Yuko</creator><creator>Fujita, Eriko</creator><creator>Hayashi, Yukiko K.</creator><creator>Zhu, Xinran</creator><creator>Lubbert, Hermann</creator><creator>Mezaki, Yoshihiro</creator><creator>Senoo, Haruki</creator><creator>Momoi, Takashi</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>201307</creationdate><title>Synaptic adhesion molecules in Cadm family at the neuromuscular junction</title><author>Tanabe, Yuko ; Fujita, Eriko ; Hayashi, Yukiko K. ; Zhu, Xinran ; Lubbert, Hermann ; Mezaki, Yoshihiro ; Senoo, Haruki ; Momoi, Takashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5032-d241d6cc263f994dbdde2e2f05985d364dd1177d1f3c0e48976c265dc77f8e7f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Bungarotoxins - metabolism</topic><topic>Cadm1</topic><topic>Cadm4</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Adhesion Molecule-1</topic><topic>Cell Adhesion Molecules - chemistry</topic><topic>Cell Adhesion Molecules - genetics</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Immunoglobulins - chemistry</topic><topic>Immunoglobulins - genetics</topic><topic>Immunoglobulins - metabolism</topic><topic>Immunohistochemistry</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mupp1</topic><topic>Muscle, Skeletal - metabolism</topic><topic>neuromuscular junction</topic><topic>Neuromuscular Junction - metabolism</topic><topic>PDZ</topic><topic>PDZ Domains</topic><topic>Protein Binding</topic><topic>Recombinant Fusion Proteins - analysis</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tanabe, Yuko</creatorcontrib><creatorcontrib>Fujita, Eriko</creatorcontrib><creatorcontrib>Hayashi, Yukiko K.</creatorcontrib><creatorcontrib>Zhu, Xinran</creatorcontrib><creatorcontrib>Lubbert, Hermann</creatorcontrib><creatorcontrib>Mezaki, Yoshihiro</creatorcontrib><creatorcontrib>Senoo, Haruki</creatorcontrib><creatorcontrib>Momoi, Takashi</creatorcontrib><collection>Istex</collection><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>Cell biology international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tanabe, Yuko</au><au>Fujita, Eriko</au><au>Hayashi, Yukiko K.</au><au>Zhu, Xinran</au><au>Lubbert, Hermann</au><au>Mezaki, Yoshihiro</au><au>Senoo, Haruki</au><au>Momoi, Takashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synaptic adhesion molecules in Cadm family at the neuromuscular junction</atitle><jtitle>Cell biology international</jtitle><addtitle>Cell Biol Int</addtitle><date>2013-07</date><risdate>2013</risdate><volume>37</volume><issue>7</issue><spage>731</spage><epage>736</epage><pages>731-736</pages><issn>1065-6995</issn><eissn>1095-8355</eissn><abstract>RA175/SynCAM1/Cadm1 (Cadm1), a member of the immunoglobulin superfamily, is a synaptic cell adhesion molecule that has a PDZ‐binding motif at the C‐terminal region. It promotes the formation of presynaptic terminals and induces functional synapses in the central nervous system. Cadm1‐deficient (knockout [KO]) mice show behavioral abnormalities, including excessive aggression and anxiety, but do not show any symptoms of neuromuscular disorder, although neuromuscular junctions (NMJs) have structures similar to synapses. We have examined the expression of members of the Cadm family in the mouse muscle tissues. Cadm4 and Cadm1 were major components of the Cadm family, and Cadm3 was faintly detected, but Cadm2 was not detected by RT‐PCR. Cadm4 as well as Cadm1 colocalized with alpha‐bungarotoxin at the NMJs and interacted with the multiple PDZ domain protein Mupp1. Cadm4 was expressed in Cadm1‐KO mice and might compensate for Cadm1 loss through interactions with Mupp1.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>23505055</pmid><doi>10.1002/cbin.10092</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals Bungarotoxins - metabolism Cadm1 Cadm4 Carrier Proteins - metabolism Cell Adhesion Molecule-1 Cell Adhesion Molecules - chemistry Cell Adhesion Molecules - genetics Cell Adhesion Molecules - metabolism Immunoglobulins - chemistry Immunoglobulins - genetics Immunoglobulins - metabolism Immunohistochemistry Mice Mice, Knockout Mupp1 Muscle, Skeletal - metabolism neuromuscular junction Neuromuscular Junction - metabolism PDZ PDZ Domains Protein Binding Recombinant Fusion Proteins - analysis Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism |
| title | Synaptic adhesion molecules in Cadm family at the neuromuscular junction |
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