title: Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain.
abstract: Striatin is an intracellular protein characterized by four protein-protein interaction domains, a caveolin-binding motif, a coiled-coil structure, a calmodulin-binding domain, and a WD repeat domain, suggesting that it is a signaling or a scaffold protein. Down-regulation of striatin, which is expressed in a few subsets of neurons, impairs the growth of dendrites as well as rat locomotor activity (Bartoli, M., Ternaux, J. P., Forni, C., Portalier, P., Salin, P., Amalric, M., and Monneron, A. (1999) J. Neurobiol. 40, 234-243). Zinedin, a "novel" protein described here, and SG2NA share with striatin identical protein-protein interaction domains and the same overall domain structure. A phylogenetic analysis supports the hypothesis that they constitute a multigenic family deriving from an ancestral gene. DNA probes and antibodies raised against specific domains of each protein showed that zinedin is mainly expressed in the central nervous system, whereas SG2NA, of more widespread occurrence, is mainly expressed in the brain and muscle. All three proteins are both cytosolic and membrane-bound. All three bind calmodulin in the presence of Ca(2+). In rat brain, SG2NA and striatin are generally not found in the same neurons. Both localize to the soma and dendrites, suggesting that they share a similar type of addressing and closely related functions.
authors.affiliation: FRE 9041, CNRS, 31 chemin Joseph Aiguier, Université de la Méditerranée, Marseille, 13402 Marseille Cedex 20, France.
authors.forename: F
authors.initials: F
authors.lastname: Castets
authors.forename: T
authors.initials: T
authors.lastname: Rakitina
authors.forename: S
authors.initials: S
authors.lastname: Gaillard
authors.forename: A
authors.initials: A
authors.lastname: Moqrich
authors.forename: M G
authors.initials: MG
authors.lastname: Mattei
authors.forename: A
authors.initials: A
authors.lastname: Monneron
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001324:Autoantigens / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology*; D001483:Base Sequence; D015152:Blotting, Northern; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology*; D002384:Catalysis; D002846:Chromatography, Affinity; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D016208:Databases, Factual; D005982:Glutathione Transferase / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D017404:In Situ Hybridization, Fluorescence; D008297:Male; D008565:Membrane Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010802:Phylogeny; D011485:Protein Binding; D051381:Rats; D011993:Recombinant Fusion Proteins; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
chemical_list: D001324:Autoantigens; D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D011993:Recombinant Fusion Proteins; C491925:STRN protein, human; C405682:STRN3 protein, human; C114095:Strn protein, rat; C485774:Strn3 protein, rat; C411649:zinedin; D005982:Glutathione Transferase; D010749:Phosphoprotein Phosphatases; D002118:Calcium