Biochemical and Biophysical Research Communications
Regular ArticlePhosphorylation of Rabphilin-3A, a Putative Target Protein for Rab3A, by Cyclic AMP-Dependent Protein Kinase
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2023, Molecular and Cellular ProteomicsCa<sup>2+</sup> sensor proteins in spontaneous release and synaptic plasticity: Limited contribution of Doc2c, rabphilin-3a and synaptotagmin 7 in hippocampal glutamatergic neurons
2021, Molecular and Cellular NeuroscienceCitation Excerpt :A null model for Doc2c has not yet been described. Rabphilin-3A, encoded by the gene Rph3a, was first identified and isolated as a putative target of Rab3a (Shirataki et al., 1993), a small G-protein involved in vesicle trafficking and neurotransmitter release (Numata et al., 1994; Shirataki et al., 1994; Takahashi et al., 1995). Electron microscopy, subcellular fractionation and imaging revealed that rabphilin-3a is transiently recruited to presynaptic vesicles (Mizoguchi et al., 1994) where it reversibly interacts with Rab3a (Stahl et al., 1996).
Deletion of synapsins I and II genes alters the size of vesicular pools and rabphilin phosphorylation
2006, Brain ResearchCitation Excerpt :One such specificity concern is whether ablation of a major phosphoprotein of the synaptic vesicle changes the phosphorylation profile of other synaptic vesicle proteins. Thus, we assessed the phosphorylation of the 234S residue of rabphilin, a protein that associates with synaptic vesicles through its binding to Rab3, and like synapsins, it is a target for protein kinase A (Numata et al., 1994; Fykse et al., 1995; Lonart and Südhof, 2001; Lonart et al., 2003; Foletti et al., 2001) and possibly for CaMKII-dependent phosphorylation (Kato et al., 1994; Foletti et al., 2001). We confirmed previous findings that rabphilin level was slightly reduced in DKO brains (Rosahl et al., 1995).
Characterization of rabphilin phosphorylation using phospho-specific antibodies
2001, NeuropharmacologyRabphilin-3: A target molecule for Rab3 small G proteins
2001, Methods in EnzymologyCasein secretion in mammary tissue: Tonic regulation of basal secretion by protein kinase A
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