Proteomics

Dataset Information

0

Phosphoproteomics of MuSK Signaling

ABSTRACT: The development of the neuromuscular synapse depends on signaling processes which involve protein phosphorylation as a crucial regulatory event. The receptor tyrosine kinase MuSK is the key signaling molecule at the neuromuscular synapse whose activity is required for the formation of a mature and functional neuromuscular synapse. However, the signaling cascade downstream of MuSK and the regulation of the different components is still poorly understood. Here we present data from a quantitative phosphoproteomics approach to study MuSK-dependent processes. Muscle cells were stimulated with the heparansulfate proteoglycan agrin, which activates MuSK and downstream signaling events. To get an insight into the signaling dynamics we used three different time points (unstimulated, 15 min, 60 min and 4 hrs).

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Myotube

SUBMITTER: Gerhard Dürnberger  

LAB HEAD: Karl Mechtler

PROVIDER: PXD000558 | Pride | 2014-06-05

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
MuSK_phosphoproteomics.msf Msf
MuSK_phosphoproteomics.pep.xml Pepxml
frac_10.raw Raw
frac_100.raw Raw
frac_101.raw Raw
Items per page:
1 - 5 of 126
altmetric image

Publications

Global analysis of muscle-specific kinase signaling by quantitative phosphoproteomics.

Dürnberger Gerhard G   Camurdanoglu Bahar Z BZ   Tomschik Matthias M   Schutzbier Michael M   Roitinger Elisabeth E   Hudecz Otto O   Mechtler Karl K   Herbst Ruth R  

Molecular & cellular proteomics : MCP 20140604 8

The development of the neuromuscular synapse depends on signaling processes that involve protein phosphorylation as a crucial regulatory event. Muscle-specific kinase (MuSK) is the key signaling molecule at the neuromuscular synapse whose activity is required for the formation of a mature and functional synapse. However, the signaling cascade downstream of MuSK and the regulation of the different components are still poorly understood. In this study we used a quantitative phosphoproteomics appro  ...[more]