Referenced in: none

Automatically associated channels: Cav2.2

Title: SUMOylation alters CRMP2 regulation of calcium influx in sensory neurons.

Authors: Weina Ju, Qi Li, Sarah M Wilson, Joel M Brittain, Louay Meroueh, Rajesh Khanna

Journal, date & volume: Channels (Austin), 2013 May-Jun , 7, 153-9

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/23510938

Abstract
The axon/dendrite specification collapsin response mediator protein 2 (CRMP2) bidirectionally modulates N-type voltage-gated Ca ( 2+) channels (CaV2.2). Here we demonstrate that small ubiquitin-like modifier (SUMO) protein modifies CRMP2 via the SUMO E2-conjugating enzyme Ubc9 in vivo. Removal of a SUMO conjugation site KMD in CRMP2 (K374A/M375A/D376A; CRMP2AAA) resulted in loss of SUMOylated CRMP2 without compromising neurite branching, a canonical hallmark of CRMP2 function. Increasing SUMOylation levels correlated inversely with calcium influx in sensory neurons. CRMP2 deSUMOylation by SUMO proteases SENP1 and SENP2 normalized calcium influx to those in the CRMP2AAA mutant. Thus, our results identify a novel role for SUMO modification in CRMP2/CaV2.2 signaling pathway.