The cytotoxic T cell proteome and its shaping by the kinase mTOR View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-01

AUTHORS

Jens L Hukelmann, Karen E Anderson, Linda V Sinclair, Katarzyna M Grzes, Alejandro Brenes Murillo, Phillip T Hawkins, Len R Stephens, Angus I Lamond, Doreen A Cantrell

ABSTRACT

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 phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3) by mTORC1 in CTLs. mTORC1 repressed PtdIns(3,4,5)P3 production and determined the requirement for mTORC2 in activation of the kinase Akt. Our unbiased proteomic analysis thus provides comprehensive understanding of CTL identity and the control of CTL function by mTORC1. More... »

PAGES

104-112

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ni.3314

    DOI

    http://dx.doi.org/10.1038/ni.3314

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1053085456

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/26551880


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