Zinedin, SG2NA, and Striatin Are Calmodulin-binding, WD Repeat Proteins Principally Expressed in the Brain

• Published in: The Journal of biological chemistry Vol. 275; no. 26; pp. 19970 - 19977
• Main Authors: Castets, Francis, Rakitina, Tatiana, Gaillard, Stéphane, Moqrich, Abdelaziz, Mattei, Marie-Geneviève, Monneron, Ariane
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30-06-2000; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Animals; Autoantigens - biosynthesis; Autoantigens - genetics; Autoantigens - physiology; Base Sequence; Blotting, Northern; Blotting, Western; Brain - metabolism; Calcium - metabolism; Calmodulin - metabolism; Calmodulin-Binding Proteins - biosynthesis; Calmodulin-Binding Proteins - genetics; Calmodulin-Binding Proteins - physiology; Catalysis; Chromatography, Affinity; Chromosome Mapping; Cloning, Molecular; Databases, Factual; Glutathione Transferase - metabolism; Humans; Immunohistochemistry; In Situ Hybridization, Fluorescence; Male; Membrane Proteins - biosynthesis; Membrane Proteins - genetics; Membrane Proteins - physiology; Molecular Sequence Data; Nerve Tissue Proteins - biosynthesis; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - physiology; Phosphoprotein Phosphatases - metabolism; Phylogeny; Protein Binding; Rats; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; SG2NA protein; Striatin; Tissue Distribution; Zinedin
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M909782199

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 Ca2+. 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.