SUMOylation alters CRMP2 regulation of calcium influx in sensory neurons

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

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

The axon/dendrite specification collapsin response mediator protein 2 (CRMP2) bidirectionally modulates N-type voltagegated 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; 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 de SUMOylation 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.

Original languageEnglish (US)
Pages (from-to)153-159
Number of pages7
JournalChannels
Volume7
Issue number3
DOIs
StatePublished - 2013
Externally publishedYes

Keywords

  • CRMP2
  • CaV2.2
  • Calcium influx
  • SUMO
  • Sensory neurons
  • Ubc9

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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