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Expression of V100 with a mutated Ca M-binding site at low levels leads to incomplete rescue of the neuronal function, and high levels of expression lead to cell death.

Our data uncover a critical regulatory function of Ca M that controls genetically separable V100 and possibly V-ATPase functions.

Moreover, in the endocytic degradative pathway, subunit a2 has recently been shown to exert another function independent of proton pumping; subunit a2 interacts with the guanine nucleotide-exchange factor ARNO in a p H-dependent manner, suggesting its function as a p H sensor for controlling the recruitment of the GTPase activated by ARNO, Arf6, which in turn directly interacts with the V-dependent, high affinity manner.

Ablation of this binding site results in a loss of Ca M recruitment to synapses.

At least two independent transgene insertions per chromosome were isolated, mapped, and tested for expression in photoreceptors using GMR-Gal4 (16) and an anti-V100 polyclonal antibody (8).

in mutant backgrounds were performed as described previously (8).

The molecular mechanisms of how the V 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.

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.

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