Proteomics

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APEX2 proximity labeling of PI(3)P dependent ER and early endosome membrane contact tether proteins

ABSTRACT: To understand the nature of ER and early endosome membrane contact site, we capitalized the MTM1 knock out (KO) HeLa cells that do not dissociate the ER and early endosome membrane contact upon nutrient starvation. By using the Doxycyclin inducible APEX2 fused Rab5A (early endosome marker) expressing stable cell lines of wildtype (WT) or KO cells, early endsome proximity proteins were acutely biotinyated during starvation. Subsequent biochemical fractionation were conducted to enrich ER membrane and biotinylated proteins were furhter enriched for Mass spectrometry analysis.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Wonyul Jang  

LAB HEAD: Volker Haucke

PROVIDER: PXD033846 | Pride | 2023-01-06

REPOSITORIES: Pride

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Publications

Endosomal lipid signaling reshapes the endoplasmic reticulum to control mitochondrial function.

Jang Wonyul W   Puchkov Dmytro D   Samsó Paula P   Liang YongTian Y   Nadler-Holly Michal M   Sigrist Stephan J SJ   Kintscher Ulrich U   Liu Fan F   Mamchaoui Kamel K   Mouly Vincent V   Haucke Volker V  

Science (New York, N.Y.) 20221216 6625

Cells respond to fluctuating nutrient supply by adaptive changes in organelle dynamics and in metabolism. How such changes are orchestrated on a cell-wide scale is unknown. We show that endosomal signaling lipid turnover by MTM1, a phosphatidylinositol 3-phosphate [PI(3)P] 3-phosphatase mutated in X-linked centronuclear myopathy in humans, controls mitochondrial morphology and function by reshaping the endoplasmic reticulum (ER). Starvation-induced endosomal recruitment of MTM1 impairs PI(3)P-de  ...[more]

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