Literature DB >> 23510938

SUMOylation alters CRMP2 regulation of calcium influx in sensory neurons.

Weina Ju1, Qi Li, Sarah M Wilson, Joel M Brittain, Louay Meroueh, Rajesh Khanna.   

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.

Entities:  

Keywords:  CRMP2; CaV2.2; SUMO; Ubc9; calcium influx; sensory neurons

Mesh：

Substances：

Year:  2013        PMID： 23510938      PMCID： PMC3710342          DOI： 10.4161/chan.24224

Source DB:  PubMed          Journal:  Channels (Austin)        ISSN： 1933-6950            Impact factor:   2.581


  50 in total

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  19 in total

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Review 10.  SUMOylation of synaptic and synapse-associated proteins: An update.

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