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Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins.

Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Research Abstract Details 

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  • Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Abstract Text:

    davide comolettiDavide Comoletti,robyn e flynnRobyn E Flynn,antony a boucardAntony A Boucard,borries demelerBorries Demeler,virgil schirfVirgil Schirf,jianxin shiJianxin Shi,lori l jenningsLori L Jennings,helen r newlinHelen R Newlin,thomas c Thomas C ,palmer taylorPalmer Taylor,

    Neuroligins 1-4 are postsynaptic transmembrane proteins capable of initiating presynaptic maturation via interactions with beta-neurexin. Both neuroligins and beta-neurexins have alternatively spliced inserts in their extracellular domains. Using analytical ultracentrifugation, we determined that the extracellular domains of the neuroligins sediment as dimers, whereas the extracellular domains of the beta-neurexins appear monomeric. Sedimentation velocity experiments of titrated stoichiometry ratios of beta-neurexin and neuroligin suggested a 2:2 complex formation. The recognition properties of individual neuroligins toward beta-neurexin-1 (NX1beta), along with the influence of their splice inserts, were explored by surface plasmon resonance and affinity chromatography. Different neuroligins display a range of NX1beta affinities spanning more than 2 orders of magnitude. Whereas splice insert 4 in beta-neurexin appears to act only as a modulator of the neuroligin/beta-neurexin association, splice insert B in neuroligin-1 (NL1) is the key element regulating the NL1/NX1beta binding. Our data indicate that gene selection, mRNA splicing, and post-translational modifications combine to give rise to a controlled neuroligin recognition code with a rank ordering of affinities for particular neurexins that is conserved for the neuroligins across mammalian species.

    Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Publishing Authors By Initials

    d comolettiD Comoletti,re flynnRE Flynn,aa boucardAA Boucard,b demelerB Demeler,v schirfV Schirf,j shiJ Shi,ll jenningsLL Jennings,hr newlinHR Newlin,tc TC ,p taylorP Taylor,

    For similar genetic phenomena: variation (genetics) research abstracts see: genetic phenomena: variation (genetics) research

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    Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Biochemistry

    VOLUME: 45

    Page Numbers: 12816-27

    Journal Abbreviation: Biochemistry

    ISSN: 0006-2960

    DAY: 24

    MONTH: Oct

    YEAR: 2006

    Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 370623

    Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Keywords Mesh Terms:

    KEYWORDS: Variation (Genetics)

    MESH TERMS: genetics

    Chemical & Substance for Abstract: Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Information

    Substance Name: neurexin Ibeta

    Registry Number: 156532-80-8

    Grant and Affiliation Information for Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins.

    AFFILIATION: Department of Pharmacology, University of California-San Diego, La Jolla, California 92093-0636, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIMH

    GRANT: R37 MH52804-08

    ACRONYM: MH

    MEDLINETA: Biochemistry

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