High impact information on Vha26

• As the ultimate target is the V-ATPase in the apical plasma membrane, this selective activation of mitochondria is clearly adaptive [1].
• The results highlight the dynamic nature and both spatial and temporal heterogeneity of calcium signaling possible in differentiated, organotypic cells and provide a new model for neuroendocrine control of V-ATPase [1].
• Lethality of these alleles could be reverted by transformation of flies with a wild type vha55::GFP fusion, confirming that the lethal phenotype described for these alleles was due to defects in V-ATPase function [2].
• One enhancer trap revealed expression of the gene encoding the C subunit of vacuolar ATPase (V-ATPase) in the medial cells of the ring gland, which produce the juvenile hormone that controls progression through developmental stages [3].
• Molecular genetic analysis of V-ATPase function in Drosophila melanogaster [4].

Biological context of Vha26

• Involvement of V-ATPase in the regulation of cell size in the fly's visual system [5].
• The vacuolar H+-ATPase (V-ATPase) is a multisubunit enzyme that couples ATP hydrolysis to proton pumping across membranes [6].

Anatomical context of Vha26

• While yeast is the model of choice for the rapid generation and identification of V-ATPase mutants, it does not allow their analysis in a plasma membrane context [4].
• Moreover, vacuolar-type H+-ATPase (V-ATPase) in the optic lobe is thought also to participate in such regulation [5].
• In the visual systems of both fly species V-ATPase was localized immunocytochemically to the compound eye photoreceptors [5].
• V-ATPase were detected in various cytoplasmic vesicles and in yolk spheres and, beginning with stage 10, also in apical follicle-cell membranes and in the oolemma [7].
• Na,K-ATPase and V-ATPase in ovarian follicles of Drosophila melanogaster [7].

Other interactions of Vha26

• Characterisation of vha26, the Drosophila gene for a 26 kDa E-subunit of the vacuolar ATPase [8].

References