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Solubility and subcellular localization of the three Drosophila RDGC phosphatase variants are determined by acylation
Author(s) -
Strauch Lisa,
Pfannstiel Jens,
Huber Armin,
Voolstra Olaf
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13163
Subject(s) - rhodopsin , phosphatase , subfamily , subcellular localization , biology , phosphoprotein , biochemistry , phosphorylation , retinal degeneration , drosophila melanogaster , microbiology and biotechnology , retinal , gene
Protein phosphorylation is an abundant molecular switch that regulates a multitude of cellular processes. In contrast to other subfamilies of phosphoprotein phosphatases, the PPEF subfamily is only poorly investigated. Drosophila retinal degeneration C ( RDGC ) constitutes the founding member of the PPEF subfamily. RDGC dephosphorylates the visual pigment rhodopsin and the ion channel TRP .However, rdgC null mutant flies exhibit rhodopsin and TRP hyperphosphorylation, altered photoreceptor physiology, and retinal degeneration. Here, we report the identification of a third RDGC protein variant and show that the three RDGC isoforms harbor different N‐termini that determine solubility and subcellular targeting due to fatty acylation. Taken together, solubility and subcellular targeting of RDGC splice variants are determined by their N‐termini.