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Protein and peptide turnover measurements using pulsed SILAC-TMT approach

ABSTRACT: We evaluated the feasibility of a workflow combining dynamic SILAC experiments with tandem mass tag (TMT)-labeling of ten pulse time-points. Replicate analysis established that the same reproducibility of turnover rates can be obtained for peptides as for proteins facilitating proteoform resolved investigation of protein stability.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell Of Cervix

SUBMITTER: Jana Zecha

LAB HEAD: Bernhard Kuster

PROVIDER: PXD008579 | Pride | 2018-02-09

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	4Replicates_pSILACTMT.zip	Other
	MQ_1.5.5.1.zip	Other
	MS1vsMS3.zip	Other
	MS2_bRP1_SILAC_TMT10.raw	Raw
	MS2_bRP2_SILAC_TMT10.raw	Raw

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Publications

Peptide Level Turnover Measurements Enable the Study of Proteoform Dynamics.

Zecha Jana J Meng Chen C Zolg Daniel Paul DP Samaras Patroklos P Wilhelm Mathias M Kuster Bernhard B

Molecular & cellular proteomics : MCP 20180202 5

The coordination of protein synthesis and degradation regulating protein abundance is a fundamental process in cellular homeostasis. Today, mass spectrometry-based technologies allow determination of endogenous protein turnover on a proteome-wide scale. However, standard dynamic SILAC (Stable Isotope Labeling in Cell Culture) approaches can suffer from missing data across pulse time-points limiting the accuracy of such analysis. This issue is of particular relevance when studying protein stabili ...[more]

PMID: 29414762

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