These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Role of the internal Shank-binding segment of glutamate receptor delta2 in synaptic localization and cerebellar functions.
    Author: Yasumura M, Uemura T, Yamasaki M, Sakimura K, Watanabe M, Mishina M.
    Journal: Neurosci Lett; 2008 Mar 12; 433(2):146-51. PubMed ID: 18249497.
    Abstract:
    Glutamate receptor (GluR) delta2 selectively expressed in cerebellar Purkinje cells (PCs) plays key roles in cerebellar long-term depression (LTD), motor learning and formation of parallel fiber (PF)-PC synapses. We have recently shown that the PDZ [postsynaptic density (PSD)-95/Discs large/zona occludens-1]-binding domain at the C-terminal, the T site, is essential for LTD induction and the regulation of climbing fiber (CF) territory, but is dispensable for synaptic localization of GluRdelta2, PF-PC synapse formation and CF elimination process. To investigate the functional roles of the S segment, the second PDZ-binding domain in the middle of the C-terminal cytoplasmic region, we generated GluRdelta2DeltaS mice carrying mutant GluRdelta2 lacking this segment. The amount of GluRdelta2DeltaS in mutant mice was reduced compared with that of GluRdelta2 in wild-type mice. However, the extent of decrease was much larger in the PSD fractions than in cerebellar homogenates, suggesting the requirement of the S segment for efficient synaptic localization. Furthermore, mismatched PF synapses and free spines emerged and CF-innervation territory on PC dendrites expanded in GluRdelta2DeltaS mice. On the other hand, the performance in the rotarod test was comparable between wild-type and GluRdelta2DeltaS mice. These results suggest that the S segment and T site, the two PDZ-binding domains in the C-terminal cytoplasmic region, are differentially involved in diverse GluRdelta2 functions.
    [Abstract] [Full Text] [Related] [New Search]