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<title lang=en>Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms</title>
<creator>Colinet, Hervé</creator>
<creator>Pineau, Charles</creator>
<creator>Com, Emmanuelle</creator>
<contributor>Ecosystèmes, biodiversité, évolution [Rennes] (ECOBIO) ; Université de Rennes 1 (UR1) - INEE - Observatoire des Sciences de l'Univers de Rennes (OSUR) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Proteomics Core Facility (Protim) ; Université de Rennes 1 (UR1) - Plateforme Génomique Santé Biogenouest®</contributor>
<contributor>actions incitatives "defis scientifiques emergents" from University of Rennes1 and SUZUKILL project [ANR-15-CE21-0017-01, FWF I 2604-B25]</contributor>
<contributor> Biogenouest</contributor>
<contributor> Conseil Regional de Bretagne</contributor>
<contributor> IBiSA</contributor>
<description>International audience</description>
<source>ISSN: 2045-2322</source>
<source>EISSN: 2045-2322</source>
<source>Scientific Reports</source>
<publisher>Nature Publishing Group</publisher>
<identifier>hal-01532256</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01532256</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01532256</source>
<source>Scientific Reports, Nature Publishing Group, 2017, 7, pp.1713 〈10.1038/s41598-017-01974-z〉</source>
<identifier>DOI : 10.1038/s41598-017-01974-z</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-017-01974-z</relation>
<identifier>PUBMED : 28490779</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/28490779</relation>
<language>en</language>
<subject>[SDE.BE] Environmental Sciences/Biodiversity and Ecology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>The regulatory mechanisms involved in the acquisition of thermal tolerance are unknown in insects. Reversible phosphorylation is a widespread post-translational modification that can rapidly alter proteins function(s). Here, we conducted a large-scale comparative screening of phosphorylation networks in adult Drosophila flies that were cold-acclimated versus control. Using a modified SIMAC method followed by a multiple MS analysis strategy, we identified a large collection of phosphopeptides (about 1600) and phosphoproteins (about 500) in both groups, with good enrichment efficacy (80%). The saturation curves from the four biological replicates revealed that the phosphoproteome was rather well covered under our experimental conditions. Acclimation evoked a strong phosphoproteomic signal characterized by large sets of unique and differential phosphoproteins. These were involved in several major GO superclusters of which cytoskeleton organization, positive regulation of transport, cell cycle, and RNA processing were particularly enriched. Data suggest that phosphoproteomic changes in response to acclimation were mainly localized within cytoskeletal network, and particularly within microtubule associated complexes. This study opens up novel research avenues for exploring the complex regulatory networks that lead to acquired thermal tolerance.</description>
<date>2017</date>
<contributor>ANR : SUZUKILL, ANR-15-CE21-0017-01</contributor>
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