Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms

Abstract 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 phosphorylatio...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Hervé Colinet, Charles Pineau, Emmanuelle Com
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a02e1e4d098845c4af39c6a52d37bb89
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:a02e1e4d098845c4af39c6a52d37bb89
record_format	dspace
spelling	oai:doaj.org-article:a02e1e4d098845c4af39c6a52d37bb892021-12-02T16:06:10ZLarge scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms10.1038/s41598-017-01974-z2045-2322https://doaj.org/article/a02e1e4d098845c4af39c6a52d37bb892017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01974-zhttps://doaj.org/toc/2045-2322Abstract 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.Hervé ColinetCharles PineauEmmanuelle ComNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hervé Colinet Charles Pineau Emmanuelle Com Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms
description	Abstract 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.
format	article
author	Hervé Colinet Charles Pineau Emmanuelle Com
author_facet	Hervé Colinet Charles Pineau Emmanuelle Com
author_sort	Hervé Colinet
title	Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms
title_short	Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms
title_full	Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms
title_fullStr	Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms
title_full_unstemmed	Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms
title_sort	large scale phosphoprotein profiling to explore drosophila cold acclimation regulatory mechanisms
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/a02e1e4d098845c4af39c6a52d37bb89
work_keys_str_mv	AT hervecolinet largescalephosphoproteinprofilingtoexploredrosophilacoldacclimationregulatorymechanisms AT charlespineau largescalephosphoproteinprofilingtoexploredrosophilacoldacclimationregulatorymechanisms AT emmanuellecom largescalephosphoproteinprofilingtoexploredrosophilacoldacclimationregulatorymechanisms
_version_	1718385106878464000

Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms

Ejemplares similares