Journal
CHANNELS
Volume 7, Issue 3, Pages 153-159Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/chan.24224
Keywords
SUMO; CRMP2; Ubc9; CaV2.2; calcium influx; sensory neurons
Categories
Funding
- Indiana Clinical and Translational Sciences Institute
- National Institutes of Health (NIH), National Center for Research Resources, Clinical and Translational Sciences Award [RR025761]
- Indiana State Department of Health-Spinal Cord and Brain Injury Fund [A70-9-079138]
- National Scientist Development grant from the American Heart Association [SDG5280023]
- Neurofibromatosis New Investigator Award from the Department of Defense Congressionally Directed Military Medical Research and Development Program [NF1000099]
- Ralph and Grace Showalter Trust Foundation award
- Stark Medical Neuroscience Fellowship
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The axon/dendrite specification collapsin response mediator protein 2 (CRMP2) bidirectionally modulates N-type voltage-gated Ca2+ 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; CRMP2(AAA)) 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 CRMP2(AAA) mutant. Thus, our results identify a novel role for SUMO modification in CRMP2/CaV2.2 signaling pathway.
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