title: Metabotropic action of postsynaptic kainate receptors triggers hippocampal long-term potentiation.
abstract: Long-term potentiation (LTP) in the rat hippocampus is the most extensively studied cellular model for learning and memory. Induction of classical LTP involves an NMDA-receptor- and calcium-dependent increase in functional synaptic AMPA receptors, mediated by enhanced recycling of internalized AMPA receptors back to the postsynaptic membrane. Here we report a physiologically relevant NMDA-receptor-independent mechanism that drives increased AMPA receptor recycling and LTP. This pathway requires the metabotropic action of kainate receptors and activation of G protein, protein kinase C and phospholipase C. Like classical LTP, kainate-receptor-dependent LTP recruits recycling endosomes to spines, enhances synaptic recycling of AMPA receptors to increase their surface expression and elicits structural changes in spines, including increased growth and maturation. These data reveal a new and, to our knowledge, previously unsuspected role for postsynaptic kainate receptors in the induction of functional and structural plasticity in the hippocampus.
authors.affiliation: School of Biochemistry, University of Bristol, Bristol, UK.|Institute of Physiology, Academy of Sciences, Prague, Czech Republic.|Insitute of Medical Physiology, School of Medicine, University of Belgrade, Belgrade, Serbia.
authors.forename: Milos M
authors.initials: MM
authors.lastname: Petrovic
authors.affiliation: Interdisciplinary Institute for Neuroscience, University of Bordeaux, Bordeaux, France.
authors.forename: Silvia
authors.initials: S
authors.lastname: Viana da Silva
authors.affiliation: Neuroscience Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore, India.
authors.forename: James P
authors.initials: JP
authors.lastname: Clement
authors.affiliation: Institute of Physiology, Academy of Sciences, Prague, Czech Republic.
authors.forename: Ladislav
authors.initials: L
authors.lastname: Vyklicky
authors.affiliation: Interdisciplinary Institute for Neuroscience, University of Bordeaux, Bordeaux, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Mulle
authors.affiliation: School of Biochemistry, University of Bristol, Bristol, UK.
authors.forename: Inmaculada M
authors.initials: IM
authors.lastname: González-González
authors.affiliation: School of Biochemistry, University of Bristol, Bristol, UK.
authors.forename: Jeremy M
authors.identifier: http://orcid.org/0000-0003-3589-8335
authors.initials: JM
authors.lastname: Henley
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D049229:Dendritic Spines / Q000378:metabolism; D011992:Endosomes / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D006624:Hippocampus / Q000502:physiology*; D017774:Long-Term Potentiation / Q000502:physiology*; D008297:Male; D009474:Neurons / Q000378:metabolism / Q000502:physiology; D011493:Protein Kinase C / Q000378:metabolism; D051381:Rats; D018091:Receptors, AMPA / Q000378:metabolism; D018092:Kainic Acid Receptors / Q000502:physiology*; D010738:Type C Phospholipases / Q000378:metabolism
chemical_list: D019204:GTP-Binding Proteins; D011493:Protein Kinase C; D018091:Receptors, AMPA; D018092:Kainic Acid Receptors; D010738:Type C Phospholipases