Proteomics

Dataset Information

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Identification of nutrient dependend PIK3C2B regulators


ABSTRACT: To identify factors responsible for the differential localization and activity of PIK3C2Bin the presence or absence of serum mitogens we took a quantitative functional proteomics approach based on stable isotope labeling of amino acids in cell culture (SILAC). Genome-engineered HEK293T cells endogenously expressing eGFP-PI3KC15were cultured in serum-containing or serum-deprived media containing heavy or light amino acids, and subjected to affinity capture using a GFP trap matrix and LC-MS/MS

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Alexander Wallroth  

LAB HEAD: Volker Haucke

PROVIDER: PXD014533 | Pride | 2019-10-02

REPOSITORIES: Pride

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Publications

Protein kinase N controls a lysosomal lipid switch to facilitate nutrient signalling via mTORC1.

Wallroth Alexander A   Koch Philipp A PA   Marat Andrea L AL   Krause Eberhard E   Haucke Volker V  

Nature cell biology 20190826 9


Mechanistic target of rapamycin (mTOR) kinase functions in two multiprotein complexes: lysosomal mTOR complex 1 (mTORC1) and mTORC2 at the plasma membrane. mTORC1 modulates the cell response to growth factors and nutrients by increasing protein synthesis and cell growth, and repressing the autophagy-lysosomal pathway<sup>1-4</sup>; however, dysfunction in mTORC1 is implicated in various diseases<sup>3,5,6</sup>. mTORC1 activity is regulated by phosphoinositide lipids<sup>7-10</sup>. Class I phos  ...[more]

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