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Large scale phosphoprotein profiling to unravel Drosophila cold acclimation regulatory mechanisms

ABSTRACT: In this study we compared the phosphoproteome of control and cold acclimated Drosophila melanogaster in order to unravel the cold acclimation regulation mechanisms. For this prurpose we enriched phosphopeptides from each sample using a sequential elution from IMAC strategy (SIMAC) and analyzed them with a LTQ-OrbitrapXL mass spectrometer using a combination of different fragmentation strategies (classical data dependant analysis using CID, neutral loss scanning and multi-stage activation) in order to improve the number of identified phosphopeptides.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

SUBMITTER: E Com

LAB HEAD: Charles Pineau

PROVIDER: PXD005311 | Pride | 2017-05-16

REPOSITORIES: Pride

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			Action	DRS
	279_1-1_CID.RAW	Raw
	279_1-1_MSA.RAW	Raw
	279_1-1_NL.RAW	Raw
	279_1-2_CID.RAW	Raw
	279_1-2_MSA.RAW	Raw

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Large scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms.

Colinet Hervé H Pineau Charles C Com Emmanuelle E

Scientific reports 20170510 1

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 (ab ...[more]

PMID: 28490779

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