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Journal of Neuroscience, Vol 15, 3747-3760, Copyright © 1995 by Society for Neuroscience
TRP, a protein essential for inositide-mediated Ca2+ influx is localized adjacent to the calcium stores in Drosophila photoreceptors
JA Pollock, A Assaf, A Peretz, CD Nichols, MH Mojet, RC Hardie and B Minke
Center for Light Microscopic Imaging and Biotechnology, Mellon University, Pittsburgh, Pennsylvania 15213-3890, USA.
The Drosophila transient receptor potential (trp) gene product (TRP) shows
some structural similarity to vertebrate voltage-gated Ca2+ channels. It
appears to function as a novel Ca2+ channel responsible for light
stimulated, inositol trisphosphate (InsP3)-mediated Ca2+ entry in the fly
retina. The subcellular localization of TRP protein was determined in this
study using immunohistochemical staining with anti-TRP antibody (MAb83F6).
TRP was localized to the base of the microvilli in a region adjacent to the
presumed InsP3-sensitive Ca2+ stores. This specific localization was
supported by measuring the magnitude of a TRP-dependent inward current that
results from spontaneous activation of the light-sensitive channels during
whole- cell recordings (the rundown current, RDC). We found that reduction
of the microvilli area through genetic dissection with the opsin null
mutant, ninaEora, was correlated with a pronounced enhancement of the
TRP-dependent inward current relative to wild type, suggesting that the
TRP-dependent current was not produced along the length of the microvilli.
We suggest that the functional localization of the TRP protein is on the
plasma membrane loop found along the base of the rhabdomeric microvillus.
Thus, the TRP channel may function in concert with the InsP3-sensitive Ca2+
stores.
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