@article{c1d4b367abd948e9abb7380dada1e512,
title = "The importance of protein phosphorylation for signaling and metabolism in response to diel light cycling and nutrient availability in a marine diatom",
abstract = "Diatoms are major contributors to global primary production and their populations in the modern oceans are affected by availability of iron, nitrogen, phosphate, silica, and other trace metals, vitamins, and infochemicals. However, little is known about the role of phosphorylation in diatoms and its role in regulation and signaling. We report a total of 2759 phosphorylation sites on 1502 proteins detected in Phaeodactylum tricornutum. Conditionally phosphorylated peptides were detected at low iron (n = 108), during the diel cycle (n = 149), and due to nitrogen availability (n = 137). Through a multi-omic comparison of transcript, protein, phosphorylation, and protein homology, we identify numerous proteins and key cellular processes that are likely under control of phospho-regulation. We show that phosphorylation regulates: (1) carbon retrenchment and reallocation during growth under low iron, (2) carbon flux towards lipid biosynthesis after the lights turn on, (3) coordination of transcription and translation over the diel cycle and (4) in response to nitrogen depletion. We also uncover phosphorylation sites for proteins that play major roles in diatom Fe sensing and utilization, including flavodoxin and phytotransferrin (ISIP2A), as well as identify phospho-regulated stress proteins and kinases. These findings provide much needed insight into the roles of protein phosphorylation in diel cycling and nutrient sensing in diatoms.",
keywords = "Diatom, Diel, Iron, Nitrogen stress, Phosphoproteome, Signaling",
author = "Tan, {Maxine H.} and Smith, {Sarah R.} and Hixson, {Kim K.} and Justin Tan and McCarthy, {James K.} and Kustka, {Adam B.} and Allen, {Andrew E.}",
note = "Funding Information: This study was supported by the National Science Foundation (NSF-MCB-1024913, NSF-MCB-1818390, NSF-OCE-0727997, NSF-OCE-1756884 to A.E.A.), the United States Department of Energy Genomics Science Program (DE-SC00006719 and DE-SC0008593 to A.E.A.), and Gordon and Betty Moore Foundation grant GBMF3828 to A.E.A. Acknowledgments: We would like to acknowledge Hong Zheng for her help with sample collection and processing. A portion of the research was performed using EMSL (grid.436923.9), a DOE Office of Science User Facility sponsored by the Office of Biological and Environmental Research. Dr. Vincent Bielinski, Dr. Tony Hunter and the Hunter lab were important in discussions of phosphorylation and phosphoproteins. Funding Information: Acknowledgments: We would like to acknowledge Hong Zheng for her help with sample collection and processing. A portion of the research was performed using EMSL (grid.436923.9), a DOE Office of Science User Facility sponsored by the Office of Biological and Environmental Research. Dr. Vincent Bielinski, Dr. Tony Hunter and the Hunter lab were important in discussions of phosphorylation and phosphoproteins. Funding Information: Funding: This study was supported by the National Science Foundation (NSF-MCB-1024913, NSF-MCB-1818390, NSF-OCE-0727997, NSF-OCE-1756884 to A.E.A.), the United States Department of Energy Genomics Science Program (DE-SC00006719 and DE-SC0008593 to A.E.A.), and Gordon and Betty Moore Foundation grant GBMF3828 to A.E.A. Publisher Copyright: {\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland.",
year = "2020",
month = jul,
doi = "https://doi.org/10.3390/biology9070155",
language = "English (US)",
volume = "9",
pages = "1--25",
journal = "Biology",
issn = "2079-7737",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "7",
}