Voltage-dependent anion channel (VDAC-1) is required for olfactory sensing in Caenorhabditis elegans

Takayuki Uozumi, Masayuki Hamakawa, Yu ki Deno, Nobushige Nakajo, Takaaki Hirotsu

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


The Ras-MAP kinase signaling pathway plays important roles for the olfactory reception in olfactory neurons in Caenorhabditis elegans. However, given the absence of phosphorylation targets of MAPK in the olfactory neurons, the mechanism by which this pathway regulates olfactory function is unknown. Here, we used proteomic screening to identify the mitochondrial voltage-dependent anion channel VDAC-1 as a candidate target molecule of MAPK in the olfactory system of C. elegans. We found that Amphid Wing "C" (AWC) olfactory neuron-specific knockdown of vdac-1 caused severe defects in chemotaxis toward AWC-sensed odorants. We generated a new vdac-1 mutant using the CRISPR-Cas9 system, with this mutant also showing decreased chemotaxis toward odorants. This defect was rescued by AWC-specific expression of vdac-1, indicating that functions of VDAC-1 in AWC neurons are essential for normal olfactory reception in C. elegans. We observed that AWC-specific RNAi of vdac-1 reduced AWC calcium responses to odorant stimuli and caused a decrease in the quantity of mitochondria in the sensory cilia. Behavioral abnormalities in vdac-1 knockdown animals might therefore be due to reduction of AWC response, which might be caused by loss of mitochondria in the cilia. Here, we showed that the function of VDAC-1 is regulated by phosphorylation and identified Thr175 as the potential phosphorylation site of MAP kinase.

Original languageEnglish
Pages (from-to)802-816
Number of pages15
JournalGenes to Cells
Issue number10
Publication statusPublished - Oct 2015

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology


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