V-ATPase V0 sector subunit a1 in neurons is a target of calmodulin

Wei Zhang, Dong Wang, Elzi Volk, Hugo J. Bellen, Peter Robin Hiesinger, Florante A. Quiocho

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


The V0 complex forms the proteolipid pore of a vesicular ATPase that acidifies vesicles. In addition, an independent function in membrane fusion has been suggested in vacuolar fusion in yeast and synaptic vesicle exocytosis in fly neurons. Evidence for a direct role in secretion has also recently been presented in mouse and worm. The molecular mechanisms of how the V0 components might act or are regulated are largely unknown. Here we report the identification and characterization of a calmodulin-binding site in the large cytosolic N-terminal region of the Drosophila protein V100, the neuron-specific V0 subunit a1. V100 forms a tight complex with calmodulin in a Ca2+-dependent manner. Mutations in the calmodulin-binding site in Drosophila lead to a loss of calmodulin recruitment to synapses. Neuronal expression of a calmodulin-binding deficient V100 uncovers an incomplete rescue at low levels and cellular toxicity at high levels. Our results suggest a vesicular ATPase V0-dependent function of calmodulin at synapses.

Original languageEnglish (US)
Pages (from-to)294-300
Number of pages7
JournalJournal of Biological Chemistry
Issue number1
StatePublished - Jan 4 2008

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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