Počet záznamů: 1  

Metabotropic glutamate receptor 1 splice variants mGluR1a and mGluR1b combine in mGluR1a/b dimers in vivo

  1. 1.
    0434606 - UMG-J 2015 RIV NL eng J - Článek v odborném periodiku
    Techlovská, Šárka - Chambers, Jayne Nicole - Dvořáková, Michaela - Petralia, R.S. - Wang, Y.X. - Hájková, Alena - Franková, Daniela - Prezeau, L. - Blahoš, Jaroslav
    Metabotropic glutamate receptor 1 splice variants mGluR1a and mGluR1b combine in mGluR1a/b dimers in vivo.
    Neuropharmacology. Roč. 86, November (2014), s. 329-326. ISSN 0028-3908
    Grant CEP: GA ČR GAP303/12/2408
    Institucionální podpora: RVO:68378050
    Klíčová slova: Glutamate receptors * GPCR * alternative splicing
    Kód oboru RIV: EB - Genetika a molekulární biologie
    Impakt faktor: 5.106, rok: 2014

    The assembly of two covalently linked monomers into dimeric complexes is a prerequisite for metabotropic glutamate receptor 1 (mGluR1) function. The former concept of a strictly homodimeric subunit contribution in metabotropic glutamate receptor complexes has recently been brought into question. Alternative splicing of the GRM1 gene results in expression of variants that vary within their intracellular C-termini. Here we bring evidence that the short mGluR1b variant is found preferentially in a complex with the long mGluR1a variant in the rodent brain. The mGluR1a and mGluR1b variants distribution overlaps in Purkinje cells and the two variants colocalize in their spines. However mGluR1a and mGluR1b show distinct sub-cellular localization when expressed alone in neurons. We discovered that trafficking of mGluR1b to distal dendrites is reliant on its association with mGluR1a and that the long C-terminus of mGluR1a within the mGluR1a/b dimer is necessary for trafficking of the complex.
    Trvalý link: http://hdl.handle.net/11104/0238611
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