PKC-2 Phosphorylation of UNC-18 Ser322 in AFD Neurons Regulates Temperature Dependency of Locomotion

Edwards, Mark R, Johnson, James R ORCID: 0000-0002-8849-0993, Rankin, Kimberley, Jenkins, Rosalind E, Maguire, Carl, Morgan, Alan ORCID: 0000-0002-0346-1289, Burgoyne, Robert D ORCID: 0000-0002-9219-0387 and Barclay, Jeff W (2012) PKC-2 Phosphorylation of UNC-18 Ser322 in AFD Neurons Regulates Temperature Dependency of Locomotion. JOURNAL OF NEUROSCIENCE, 32 (20). pp. 7042-7051.

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Official URL: http://dx.doi.org/10.1523/jneurosci.4029-11.2012

Abstract

Diacylglycerol (DAG)/protein kinase C (PKC) signaling plays an integral role in the regulation of neuronal function. This is certainly true in Caenorhabditis elegans and in particular for thermosensory signaling and behavior. Downstream molecular targets for transduction of this signaling cascade remain, however, virtually uncharacterized. We investigated whether PKC phosphorylation of Munc18-1, an essential protein in vesicle trafficking and exocytosis, was the downstream effector for DAG regulation of thermosensory behavior. We demonstrate here that the C. elegans ortholog of Munc18-1, UNC-18, was phosphorylated in vitro at Ser322. Transgenic rescue of unc-18-null worms with Ser322 phosphomutants displayed altered thermosensitivity. C. elegans expresses three DAG-regulated PKCs, and blocking UNC-18 Ser322 phosphorylation was phenocopied only by deletion of calcium-activated PKC-2. Expression of nonphosphorylatable UNC-18 S322A, either pan-neuronally or specifically in AFD thermosensory neurons, converted wild-type worms to a pkc-2-null phenotype. These data demonstrate that an individual DAG-dependent thermosensory behavior of an organism is effected specifically by the downstream PKC-2 phosphorylation of UNC-18 on Ser322 in AFD neurons.

Item Type:	Article
Additional Information:	## TULIP Type: Articles/Papers (Journal) ##
Uncontrolled Keywords:	Animals, Caenorhabditis elegans, Isoenzymes, Protein Kinase C, Diglycerides, Caenorhabditis elegans Proteins, Vesicular Transport Proteins, Phosphoproteins, Signal Transduction, Phosphorylation, Locomotion, Mutation, Qa-SNARE Proteins, Sensory Receptor Cells, Thermosensing
Depositing User:	Symplectic Admin
Date Deposited:	28 Apr 2016 10:15
Last Modified:	19 Jan 2023 07:37
DOI:	10.1523/JNEUROSCI.4029-11.2012
Open Access URL:	http://www.ncbi.nlm.nih.gov/pmc/articles/PMC337432...
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3000900