cDNA cloning of a neural visinin-like Ca2+-binding protein

Kuno, Toshiki; Kajimoto, Yasuo; Hashimoto, Takeshi; Mukai, Hideyuki; Shirai, Yutaka; Saheki, Shûichi; Tanaka, Chikako

doi:10.1016/s0006-291x(05)80012-9

Cited by 67 publications

(33 citation statements)

References 10 publications

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“…1A). Screening the National Institutes of Health nonredundant data base identified the coding region as visinin-like protein (VILIP) (GenBank TM accession number D21165) (19,20). VILIP is a neural Ca 2ϩ -binding protein (NCaPs) that belongs to the superfamily of EF-hand Ca 2ϩ -binding proteins (19).…”

Section: Resultsmentioning

confidence: 99%

Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Mathisen

Johnson

Kawczak

et al. 1999

Journal of Biological Chemistry

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Double-stranded RNA-binding proteins function in regulating the stability, translation, and localization of specific mRNAs. In this study, we have demonstrated that the neuron-specific, calcium-binding protein, visinin-like protein (VILIP) contains one double-stranded RNA-binding domain, a protein motif conserved among many double-stranded RNA-binding proteins. We showed that VILIP can specifically bind doublestranded RNA, and this interaction specifically requires the presence of calcium. Mobility shift studies indicated that VILIP binds double-stranded RNA as a single protein-RNA complex with an apparent equilibrium dissociation constant of 9.0 ؋ 10 ؊6 M. To our knowledge, VILIP is the first double-stranded RNA-binding protein shown to be calcium-dependent. Furthermore, VILIP specifically binds the 3-untranslated region of the neurotrophin receptor, trkB, an mRNA localized to hippocampal dendrites in an activity-dependent manner. Given that VILIP is also expressed in the hippocampus, these data suggest that VILIP may employ a novel, calcium-dependent mechanism to regulate its binding to important localized mRNAs in the central nervous system.

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Section: Resultsmentioning

confidence: 99%

Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Mathisen

Johnson

Kawczak

et al. 1999

Journal of Biological Chemistry

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“…Further analysis of this region revealed the presence of three Ca2+-binding EF-hand motifs that had the highest homology (52-54% similarity; 32-35% identity) to a family of genes belonging to visinin-like Ca2+-binding proteins (Fig. 2), found mainly in neural tissue (33)(34)(35)(36)(37). Even (Fig.…”

Section: Resultsmentioning

confidence: 99%

Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain.

Patil

Takezawa

Poovaiah

1995

Proc. Natl. Acad. Sci. U.S.A.

158

134

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“…The sequences shown are those of bovine recoverin (1), chicken visinin (6), bovine neurocalcin (7), rat 21-kDa CABP (calcium-binding protein) (8), Drosophila melanogaster frequenin (J.…”

Section: Discussionmentioning

confidence: 99%

“…Bovine recoverin is 59%o identical in amino acid sequence to visinin, a Ca2+-binding protein found in chicken cone cells (6). Homologs of recoverin and visinin have recently been found in mammalian brain (7)(8)(9)(10). Interest in this Ca2+ sensor has been further heightened by the finding that the aminoterminal glycine of retinal recoverin is linked to a myristoyl (C14:0) or related fatty acyl group (C14:1, C14:2, or C12:0) (11).…”

mentioning

confidence: 99%

Calcium-myristoyl protein switch.

Zozulya

Stryer

1992

Proc. Natl. Acad. Sci. U.S.A.

342

306

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Recoverin, a recently discovered member of the EF-hand superfamily of Ca2+-bindig proteins, serves as a Ca2+ sensor in vision. The amino terminus of the protein from retinal rod cells contains a covalently attached myristoyl or related N-acyl group. We report here studies of unmyrtylated and myristoylated recombinant recoverin designed to delineate the biological role of this hydrophobic unit. Ca2+ induces the binding of both the unmyristoylated and myristoylated proteins to phenyl-agarose, a hydrophobic support. MATERIALS AND METHODSRecoverin. Recombinant myristoylated and unmyristoylated recoverins were expressed in the overproducing E. coli strains pTrec2/pBB131/DH5aF' and pTrec2/DH5a, respectively, and were purified by a modification of a previously described procedure (5, 15). Cells from 20 liters of a bacterial culture were resuspended in 200 ml of 100 mM KCl/1 mM dithiothreitol/1 mM MgCl2/50 mM potassium Hepes, pH 7.5 (buffer A) supplied with 1 mM EGTA and disrupted by sonication. Streptomycin sulfate was added with stirring over a 10-min period to a final concentration of 0.1% from a 5% stock prepared in buffer A, and the cell debris was removed by centrifugation at 40C for 30 min at 18,000 x g. The cleared lysate was filtered through filter paper (Whatman 1), brought to 2 mM CaCl2, and applied to an 80-ml phenyl-Sepharose CL-4B (Pharmacia) column previously equilibrated with buffer A containing 2 mM CaC12. The column was washed with 400 ml of the same buffer, and the fraction containing recoverin was eluted with 100-150 ml of buffer A containing 2 mM EGTA. The eluate was diluted with 3 volumes of cold water, applied to a HiLoad 26/10 Q-Sepharose HP column (Pharmacia), and chromatographed with a gradient of 0-200 mM KCl in 500 ml of 20 mM Tris-HCl, pH 8.0/1 mM dithiothreitol/1 mM MgCl2/0.1 mM EGTA. Purified recoverin was concentrated to 10-20 mg/ml using Centriprep 10 centrifugal concentrators (Amicon), flash-frozen in liquid nitrogen, and stored at -70'C.To produce tritium-labeled myristoylated recoverin, the overproducing strain pTrec2/pBB131/DHSFa' containing the yeast N-myristoyltransferase expression vector (22) 11569The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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cDNA cloning of a neural visinin-like Ca2+-binding protein

Cited by 67 publications

References 10 publications

Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain.

Calcium-myristoyl protein switch.

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