Key role of the postsynaptic density scaffold proteins Shank and Homer in functional artchitecure of Ca2+ heomeostasis at dendritic spines in hippocampal neurons. (Articolo in rivista)

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  • Key role of the postsynaptic density scaffold proteins Shank and Homer in functional artchitecure of Ca2+ heomeostasis at dendritic spines in hippocampal neurons. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Sala C, Roussignol G, Meldolesi J, and Fagni L (2005)
    Key role of the postsynaptic density scaffold proteins Shank and Homer in functional artchitecure of Ca2+ heomeostasis at dendritic spines in hippocampal neurons.
    in The Journal of neuroscience
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Sala C, Roussignol G, Meldolesi J, and Fagni L (literal)
Pagina inizio
  • 4587 (literal)
Pagina fine
  • 4592 (literal)
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  • 25 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1Cellular and Molecular Pharmacology Section, Institute of Neuroscience, Consiglio Nazionale delle Ricerche, and Department of Pharmacology, University of Milan, 20129 Milan, Italy, 2Institut de Génomique Fonctionelle, Unité Mixte de Recherche 5203, 34094 Montpellier, France, and 3Department of Neuroscience, Vita-Salute San Raffaele University, and Center of Excellence in the Physiopathology of Cell Differentiation, 20132 Milan, Italy (literal)
Titolo
  • Key role of the postsynaptic density scaffold proteins Shank and Homer in functional artchitecure of Ca2+ heomeostasis at dendritic spines in hippocampal neurons. (literal)
Abstract
  • Akey aspect of postsynaptic function, also important for plasticity, is the segregation within dendritic spines of Ca2?rises attributable to release from intracellular stores. Previous studies have shown that overexpression in hippocampal neurons of two postsynaptic density (PSD) scaffold proteins, Shank1B and Homer1b, induces spine maturation, including translocation of the intracellular Ca2? channel inositol trisphosphate receptor (IP3R). The structural and functional significance of these processes remained undefined. Here, we show that in its relocation, IP3R is accompanied by other endoplasmic reticulum (ER) proteins: the Ca2? pump sarcoendoplasmic reticulum calcium ATPase, the lumenal Ca2?-binding protein calreticulin, the ER lumen-addressed green fluorescent protein, and, to a lesser extent, the membrane chaperone calbindin. The specificity of these translocations was demonstrated by their inhibition by both a Shank1 fragment and the dominant-negative Homer1a. Activation in Shank1B-transfected neurons of the metabotropic glutamatergic receptors 1/5 (mGluRs1/5), which induce IP3 generation with ensuing Ca2? release from the stores, triggered considerable increases in Ca2?- dependent responses: activation of the bigK?channel, which was revealed by patch clamping, and extracellular signal-regulated protein kinase (ERK) phosphorylation. The interaction of Shank1B and Homer1b appears as the molecular mechanism linking mGluRs1/5, strategically located in the spines, to IP3Rwith the integration of entire ER cisternas in the PSD and with consequences on both local Ca2? homeostasis and overall neuronal signaling. (literal)
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