title: A novel calmodulin-binding protein, belonging to the WD-repeat family, is localized in dendrites of a subset of CNS neurons.
abstract: A rat brain synaptosomal protein of 110,000 M(r) present in a fraction highly enriched in adenylyl cyclase activity was microsequenced (Castets, F., G. Baillat, S. Mirzoeva, K. Mabrouk, J. Garin, J. d'Alayer, and A. Monneron. 1994. Biochemistry. 33:5063-5069). Peptide sequences were used to clone a cDNA encoding a novel, 780-amino acid protein named striatin. Striatin is a member of the WD-repeat family (Neer, E.J., C.J. Schmidt, R. Nambudripad, and T.F. Smith. 1994. Nature (Lond.). 371:297-300), the first one known to bind calmodulin (CaM) in the presence of Ca++. Subcellular fractionation shows that striatin is a membrane-associated, Lubrol-soluble protein. As analyzed by Northern blots, in situ hybridization, and immunocytochemistry, striatin is localized in the central nervous system, where it is confined to a subset of neurons, many of which are associated with the motor system. In particular, striatin is conspicuous in the dorsal part of the striatum, as well as in motoneurons. Furthermore, striatin is essentially found in dendrites, but not in axons, and is most abundant in dendritic spines. We propose that striatin interacts, through its WD-repeat domain and in a CaM/Ca(++)-dependent manner, with one or several members of a surrounding cluster of molecules engaged in a Ca(++)-signaling pathway specific to excitatory synapses.
authors.affiliation: UPR Centre National de la Recherche Scientifique (CNRS) 9013, Laboratoire de Neurobiologie Cellulaire et Fonctionnelle, Marseille, France.
authors.forename: F
authors.initials: F
authors.lastname: Castets
authors.forename: M
authors.initials: M
authors.lastname: Bartoli
authors.forename: J V
authors.initials: JV
authors.lastname: Barnier
authors.forename: G
authors.initials: G
authors.lastname: Baillat
authors.forename: P
authors.initials: P
authors.lastname: Salin
authors.forename: A
authors.initials: A
authors.lastname: Moqrich
authors.forename: J P
authors.initials: JP
authors.lastname: Bourgeois
authors.forename: F
authors.initials: F
authors.lastname: Denizot
authors.forename: G
authors.initials: G
authors.lastname: Rougon
authors.forename: G
authors.initials: G
authors.lastname: Calothy
authors.forename: A
authors.initials: A
authors.lastname: Monneron
mesh_terms: D000262:Adenylyl Cyclases / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002148:Calmodulin-Binding Proteins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D002458:Cell Fractionation; D002490:Central Nervous System / Q000737:chemistry*; D003001:Cloning, Molecular; D003342:Corpus Striatum / Q000737:chemistry; D000242:Cyclic AMP / Q000096:biosynthesis; D018076:DNA, Complementary / Q000235:genetics; D003712:Dendrites / Q000737:chemistry*; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009046:Motor Neurons / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D017207:Rats, Sprague-Dawley; D017208:Rats, Wistar; D017421:Sequence Analysis; D017422:Sequence Analysis, DNA; D012995:Solubility
chemical_list: D002148:Calmodulin-Binding Proteins; D018076:DNA, Complementary; D010455:Peptides; D012333:RNA, Messenger; D000242:Cyclic AMP; D000262:Adenylyl Cyclases