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Teneurin Structure: Splice Variants of a Bacterial Toxin Homolog Specifies Synaptic Connections
Teneurins are a conserved family of cell-surface adhesion molecules that mediate cellular communication, and play key roles in embryonic and neural development. Their mechanisms of action remained unclear due in part to their unknown structures. In recent years, the structures of teneurins have been...
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Published in: | Frontiers in neuroscience 2019-08, Vol.13, p.838-838 |
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description | Teneurins are a conserved family of cell-surface adhesion molecules that mediate cellular communication, and play key roles in embryonic and neural development. Their mechanisms of action remained unclear due in part to their unknown structures. In recent years, the structures of teneurins have been reported at atomic resolutions and revealed a clear homology to bacterial Tc toxins with no similarity to other eukaryotic proteins. Another surprising observation was that alternatively spliced variants of teneurins interact with distinct ligands, and thus specify excitatory vs. inhibitory synapses. In this review, we discuss teneurin structures that together with structure-guided biochemical and functional analyses, provide insights for the mechanisms of trans-cellular communication at the synapse and other cell-cell contact sites. |
doi_str_mv | 10.3389/fnins.2019.00838 |
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Li, Jingxian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-9aa818f067750ffd5bcb5cbdeeef40da2b146bad04e71dc7242fbc7b86002eb83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>adhesion GPCR</topic><topic>Alternative splicing</topic><topic>Amino acids</topic><topic>Cell adhesion</topic><topic>Cell interactions</topic><topic>Cell signaling</topic><topic>Embryogenesis</topic><topic>Epidermal growth factor</topic><topic>Homology</topic><topic>Latrophilin/ADGRL</topic><topic>Neuroscience</topic><topic>ODZ</topic><topic>Proteins</topic><topic>structure</topic><topic>synapse</topic><topic>Synapses</topic><topic>teneurin</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Araç, Demet</creatorcontrib><creatorcontrib>Li, Jingxian</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>Biological Sciences</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Frontiers in neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Araç, Demet</au><au>Li, Jingxian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Teneurin Structure: Splice Variants of a Bacterial Toxin Homolog Specifies Synaptic Connections</atitle><jtitle>Frontiers in neuroscience</jtitle><addtitle>Front Neurosci</addtitle><date>2019-08-07</date><risdate>2019</risdate><volume>13</volume><spage>838</spage><epage>838</epage><pages>838-838</pages><issn>1662-4548</issn><issn>1662-453X</issn><eissn>1662-453X</eissn><abstract>Teneurins are a conserved family of cell-surface adhesion molecules that mediate cellular communication, and play key roles in embryonic and neural development. 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subjects | adhesion GPCR Alternative splicing Amino acids Cell adhesion Cell interactions Cell signaling Embryogenesis Epidermal growth factor Homology Latrophilin/ADGRL Neuroscience ODZ Proteins structure synapse Synapses teneurin Toxins |
title | Teneurin Structure: Splice Variants of a Bacterial Toxin Homolog Specifies Synaptic Connections |
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