Proteomics

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Integrative proteomics and phosphoproteomics profiling and systems biology analysis reveal dynamic signaling networks and mTORC1-dependent mitochondrial function in T cell activation


ABSTRACT: The underlying mechanisms by which naïve T cells exit from quiescence after antigen stimulation remain elusive. Using multiplex isobaric labeling proteomics technology, we report unbiased, temporal profiling of whole proteome and phosphoproteome during the activation in the wild type and Rptor-/- T cells. TCR stimulation results in dynamic reprogramming of the proteome and phosphoproteome, with predominant upregulation of molecular machineries in protein translation and mitochondrial activation. Loss of mTORC1 disrupts TCR-induced mitochondrial functions including mitoribosome biogenesis, one-carbon metabolism and oxidative phosphorylation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): T Cell

SUBMITTER: xusheng wang  

LAB HEAD: Junmin Peng, PhD

PROVIDER: PXD005492 | Pride | 2017-03-29

REPOSITORIES: Pride

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Publications

Integrative Proteomics and Phosphoproteomics Profiling Reveals Dynamic Signaling Networks and Bioenergetics Pathways Underlying T Cell Activation.

Tan Haiyan H   Yang Kai K   Li Yuxin Y   Shaw Timothy I TI   Wang Yanyan Y   Blanco Daniel Bastardo DB   Wang Xusheng X   Cho Ji-Hoon JH   Wang Hong H   Rankin Sherri S   Guy Cliff C   Peng Junmin J   Chi Hongbo H  

Immunity 20170309 3


The molecular circuits by which antigens activate quiescent T cells remain poorly understood. We combined temporal profiling of the whole proteome and phosphoproteome via multiplexed isobaric labeling proteomics technology, computational pipelines for integrating multi-omics datasets, and functional perturbation to systemically reconstruct regulatory networks underlying T cell activation. T cell receptors activated the T cell proteome and phosphoproteome with discrete kinetics, marked by early d  ...[more]

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