Proteomics

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Proteomic analysis of Raptor-proximal proteins in U2OS cells

ABSTRACT: The mammalian target of rapamycin complex 1 (mTORC1) is a key nutrient-sensing hub and a master regulator of cellular growth and metabolism. Activation of mTORC1 by amino acids and growth factors requires its recruitment to the lysosomes. Furthermore, lysosomal distribution has been shown to be intimately involved in the control of mTORC1, where localisation of lysosomes near plasma membrane increases mTORC1 activity. However, the underlying mechanisms by which lysosomal positioning impacts on mTORC1 signalling are not well understood. To understand better the spatial associations of mTORC1, we analysed the proximal ‘interactome’ of the constitutive component of mTORC1, Raptor, using BioID2-based proximity labelling and MS-based proteomics.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Osteosarcoma

SUBMITTER: Adam Byron  

LAB HEAD: Viktor I Korolchuk

PROVIDER: PXD012795 | Pride | 2021-09-08

REPOSITORIES: Pride

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Publications

The mammalian target of rapamycin complex 1 (mTORC1) integrates mitogenic and stress signals to control growth and metabolism. Activation of mTORC1 by amino acids and growth factors involves recruitment of the complex to the lysosomal membrane and is further supported by lysosome distribution to the cell periphery. Here, we show that translocation of lysosomes toward the cell periphery brings mTORC1 into proximity with focal adhesions (FAs). We demonstrate that FAs constitute discrete plasma mem  ...[more]

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