Dataset Information


Mammalian Target of Rapamycin shapes the cytotoxic T cell proteome

ABSTRACT: High resolution mass spectrometry maps the CD8 cytotoxic cell (CTL) proteome and the impact of mammalian target of rapamycin complex 1 (mTORC1) on CTL. We show mTORC1 selectively represses and promotes expression of a subset (10%) of CTL proteins including key CTL effector and adhesion molecules and adaptor proteins. mTORC1 also controls flux through a selective subset of metabolic pathways but is not an on/off switch for CTL metabolism. Proteomic data highlighted the potential for mTORC1 negative control of phosphatidylinositol (3,4,5)-trisphosphate (PI(3,4,5)P3) production in CTL. Further work revealed that mTORC1 represses PI(3,4,5)P3 production and controls the mTORC2 requirement for activation of the serine/threonine kinase AKT. Unbiased proteomic analysis thus provides a comprehensive understanding of CTL identity and mTORC1 control of CTL function.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus musculus  

TISSUE(S): Spleen

DISEASE(S): Not Available

SUBMITTER: Jens Hukelmann  

LAB HEAD: Doreen Ann Cantrell

PROVIDER: PXD002928 | Pride | 2015-10-13


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We used high-resolution mass spectrometry to map the cytotoxic T lymphocyte (CTL) proteome and the effect of the metabolic checkpoint kinase mTORC1 on CTLs. The CTL proteome was dominated by metabolic regulators and granzymes, and mTORC1 selectively repressed and promoted expression of a subset of CTL proteins (~10%). These included key CTL effector molecules, signaling proteins and a subset of metabolic enzymes. Proteomic data highlighted the potential for negative control of the production of  ...[more]

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