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.

OTHER RELATED OMICS DATASETS IN: PRJNA289932

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Spleen, Cd8-positive

SUBMITTER: Jens Hukelmann  

LAB HEAD: Doreen Ann Cantrell

PROVIDER: PXD002928 | Pride | 2015-10-13

REPOSITORIES: Pride