title: Gq protein alpha subunits Galphaq and Galpha11 are localized at postsynaptic extra-junctional membrane of cerebellar Purkinje cells and hippocampal pyramidal cells.
abstract: Following cell surface receptor activation, the alpha subunit of the Gq subclass of GTP-binding proteins activates the phosphoinositide signalling pathway. Here we examined the expression and localization of Gq protein alpha subunits in the adult mouse brain by in situ hybridization and immunohistochemistry. Of the four members of the Gq protein alpha subunits, Galphaq and Galpha11 were transcribed predominantly in the brain. The highest transcriptional level of Galphaq was observed in cerebellar Purkinje cells (PCs) and hippocampal pyramidal cells, while that of Galpha11 was noted in hippocampal pyramidal cells. Antibody against the C-terminal peptide common to Galphaq and Galpha11 strongly labelled the cerebellar molecular layer and hippocampal neuropil layers. In these regions, immunogold preferentially labelled the cytoplasmic face of postsynaptic cell membrane of PCs and pyramidal cells. Immunoparticles were distributed along the extra-junctional cell membrane of spines, dendrites and somata, but were almost excluded from the junctional membrane. By double immunofluorescence, Galphaq/Galpha11 was extensively colocalized with metabotropic glutamate receptor mGluR1alpha in dendritic spines of PCs and with mGluR5 in those of hippocampal pyramidal cells. Together with concentrated localization of mGluR1alpha and mGluR5 in a peri-junctional annulus on PC and pyramidal cell synapses (Baude et al. 1993, Neuron, 11, 771-787; Luján et al. 1996, Eur. J. Neurosci., 8, 1488-1500), the present molecular-anatomical findings suggest that peri-junctional stimulation of the group I metabotropic glutamate receptors is mediated by Galphaq and/or Galpha11, leading to the activation of the intracellular effector, phospholipase Cbeta.
authors.affiliation: Department of Anatomy, Hokkaido University School of Medicine, Sapporo 060-8638, Japan.
authors.forename: J
authors.initials: J
authors.lastname: Tanaka
authors.forename: S
authors.initials: S
authors.lastname: Nakagawa
authors.forename: E
authors.initials: E
authors.lastname: Kushiya
authors.forename: M
authors.initials: M
authors.lastname: Yamasaki
authors.forename: M
authors.initials: M
authors.lastname: Fukaya
authors.forename: T
authors.initials: T
authors.lastname: Iwanaga
authors.forename: M I
authors.initials: MI
authors.lastname: Simon
authors.forename: K
authors.initials: K
authors.lastname: Sakimura
authors.forename: M
authors.initials: M
authors.lastname: Kano
authors.forename: M
authors.initials: M
authors.lastname: Watanabe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002531:Cerebellum / Q000166:cytology / Q000378:metabolism* / Q000648:ultrastructure; D019085:Fluorescent Antibody Technique, Direct; D043802:GTP-Binding Protein alpha Subunits, Gq-G11; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D006624:Hippocampus / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D051379:Mice; D008810:Mice, Inbred C57BL; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D016376:Oligonucleotides, Antisense; D011689:Purkinje Cells / Q000378:metabolism* / Q000648:ultrastructure; D017966:Pyramidal Cells / Q000378:metabolism* / Q000648:ultrastructure; D018094:Receptors, Metabotropic Glutamate / Q000235:genetics / Q000502:physiology; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology; D013570:Synaptic Membranes / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D016376:Oligonucleotides, Antisense; D018094:Receptors, Metabotropic Glutamate; D019204:GTP-Binding Proteins; D043802:GTP-Binding Protein alpha Subunits, Gq-G11