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Signal."],"published-print":{"date-parts":[[2026,9,29]]},"abstract":"<jats:p>\n                    Light is an important environmental stimulus that is necessary for vision and circadian entrainment. Here, we present a system-wide analysis of the kinase-mediated light response in\n                    <jats:italic toggle=\"yes\">Drosophila<\/jats:italic>\n                    using optimized data-independent acquisition mass spectrometry (DIA-MS) for quantitative phosphoproteomics analysis. Exposure to standard white light or high-intensity blue light induced a widespread increase in phosphorylation relative to dark-adapted flies. The light-sensitive phosphoproteins were part of multiple pathways, including phototransduction, circadian control, lipid metabolism, and synapse organization, and exhibited distinct phosphorylation signatures under dark adaptation or white or blue light. The Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -permeable transient receptor potential (Trp) channel was differentially phosphorylated at multiple sites in a white and blue light\u2013dependent manner, and phosphorylation stoichiometric analysis identified Thr\n                    <jats:sup>849<\/jats:sup>\n                    in Trp as a pivotal functional switch. It was entirely unphosphorylated in the dark, but 80% of the Trp molecules were phosphorylated in either light condition. This phosphorylation event was mediated in part by the eye-specific protein kinase C InaC and regulated the eye\u2019s electrophysiological response to oscillating light. Thus, our results show that light remodels the\n                    <jats:italic toggle=\"yes\">Drosophila<\/jats:italic>\n                    phosphoproteome, establishing a crucial mechanism for sensory adaptation to a changing light-dark environment.\n                  <\/jats:p>","DOI":"10.1126\/scisignal.aei4151","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T17:58:26Z","timestamp":1790704706000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":1,"title":["Light-induced remodeling of the\n                    <i>Drosophila<\/i>\n                    phosphoproteome regulates visual adaptation through the Trp channel"],"prefix":"10.1126","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5360-900X","authenticated-orcid":true,"given":"Lucas D.","family":"Kramer","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-5708-176X","authenticated-orcid":true,"given":"Tal","family":"Brandwine-Shemmer","sequence":"additional","affiliation":[{"name":"Department of Medical Neurobiology Faculty of Medicine and Edmond and Lily Safra Center for Brain Sciences (ELSC), Hebrew University, Jerusalem, Israel."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leah R.","family":"Pierce","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8712-3326","authenticated-orcid":true,"given":"Yi-Kai","family":"Liu","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0055-5706","authenticated-orcid":true,"given":"Jonas-Peter","family":"Bartels","sequence":"additional","affiliation":[{"name":"Institute of Biology, Department of Biochemistry, University of Hohenheim, 70599 Stuttgart, Germany."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Armin","family":"Huber","sequence":"additional","affiliation":[{"name":"Institute of Biology, Department of Biochemistry, University of Hohenheim, 70599 Stuttgart, Germany."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7583-6556","authenticated-orcid":true,"given":"Baruch","family":"Minke","sequence":"additional","affiliation":[{"name":"Department of Medical Neurobiology Faculty of Medicine and Edmond and Lily Safra Center for Brain Sciences (ELSC), Hebrew University, Jerusalem, Israel."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5535-5517","authenticated-orcid":true,"given":"W. Andy","family":"Tao","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA."},{"name":"Purdue Center for Cancer Research, Purdue University, West Lafayette, IN 47907, USA."},{"name":"Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5933-9952","authenticated-orcid":true,"given":"Vikki M.","family":"Weake","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA."},{"name":"Purdue Center for Cancer Research, Purdue University, West Lafayette, IN 47907, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.3390\/ijms23020729"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1350-9462(98)00005-6"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cub.2005.05.058"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.3670-16.2017"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1002\/wmts.20"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.3389\/neuro.03.002.2009"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1085\/jgp.103.3.409"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","unstructured":"J. Yao P. Pang B. Gao X. Mo X. Lu X. Li P. Wang Q. Shi K. Xia P. Xiao H. Gai C. Xie D. Li D. Sun C. Tian Chemoreceptor TRP\u03b3 coordinates locomotor activity via regulating intracellular Ca2+ homeostasis in Drosophila. Research Square [Preprint] (2025); https:\/\/doi.org\/10.21203\/rs.3.rs-7403702\/v1.","DOI":"10.21203\/rs.3.rs-7403702\/v1"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2023.102723"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00359-010-0568-7"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00359-019-01397-3"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-74742-1"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/333737a0"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature22325"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.8316831"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1038\/s41514-017-0019-6"},{"key":"e_1_3_2_18_2","first-page":"394","article-title":"CULD is required for rhodopsin and TRPL channel endocytic trafficking and survival of photoreceptor cells","volume":"129","author":"Xu Y.","year":"2016","unstructured":"Y. Xu, T. Wang, CULD is required for rhodopsin and TRPL channel endocytic trafficking and survival of photoreceptor cells. J. Cell Sci. 129, 394\u2013405 (2016).","journal-title":"J. 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