ArticlePloS one2015
Light-dependent phosphorylation of the Drosophila inactivation no afterpotential D (INAD) scaffolding protein at Thr170 and Ser174 by eye-specific protein kinase C.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Light adaptation of the microvillus refractory period in blow fly photoreceptors.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2026Article
- Immunocytochemical Labeling of Rhabdomeric Proteins inThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019Article
- In vivo tracking of phosphoinositides in Drosophila photoreceptors.Journal of cell science · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein that tethers components of the phototransduction cascade to form a supramolecular signaling complex. Here, we report the identification of eight INAD phosphorylation sites using a mass spectrometry approach. PDZ1, PDZ2, and PDZ4 each harbor one phosphorylation site, three phosphorylation sites are located in the linker region between PDZ1 and 2, one site is located between PDZ2 and PDZ3, and one site is located in the N-terminal region. Using a phosphospecific antibody, we found that INAD phosphorylated at Thr170/Ser174 was located within the rhabdomeres of the photoreceptor cells, suggesting that INAD becomes phosphorylated in this cellular compartment. INAD phosphorylation at Thr170/Ser174 depends on light, the phototransduction cascade, and on eye-Protein kinase C that is attached to INAD via one of its PDZ domains.
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