PMID: 8939464Nov 1, 1996Paper

The synaptic protein UNC-18 is phosphorylated by protein kinase C

Neurochemistry International
T SassaR Hosono

Abstract

The C. elegans unc-18 encoded protein UNC-18 is implicated in the interactions between synaptic vesicles and presynaptic plasma membrane. To further characterize the neural protein, we investigated the phosphorylation in vitro of the protein expressed in Spodoptera frugiperda Sf21 cells. The UNC-18 protein is selectively phosphorylated by protein kinase C (PKC) but not by casein kinase II and cyclic AMP-dependent protein kinase. The presumed phosphorylation sites determined by manual Edman degradation were serine-2, serine-322, threonine-462 and serine-515, of which the last is highly conserved as a consensus phosphorylation site for PKC in Drosophila and the mammalian homologue. Phosphorylated UNC-18 extracted from C. elegans was also detected, indicating that it has a physiological role in intact nerve terminals. Therefore, the phosphorylation by PKC may play a physiological role in the regulation.

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Citations

Nov 1, 1996·Neurochemistry International·H OgawaR Hosono
Jan 29, 2000·The European Journal of Neuroscience·K J de VriesM Verhage
May 18, 2012·The Journal of Neuroscience : the Official Journal of the Society for Neuroscience·Mark R EdwardsJeff W Barclay
Dec 19, 2001·Yeast·M H BrummerS Keränen
Jun 27, 2018·Alcoholism, Clinical and Experimental Research·Nancy J AlexanderBrian A McCool
Jan 27, 1998·The Journal of Biological Chemistry·H OgawaR Hosono
Oct 7, 2004·Gene Expression Patterns : GEP·Mariana Leguia, Gary M Wessel
Aug 16, 2005·Cell Calcium·Jeff W BarclayRobert D Burgoyne

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