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RMDN3, a key tethering protein at ER-mitochondria contact sites, upon phosphorylation with PTPIP51, enhances the tightness of ER-mitochondria membrane contacts, acting as a molecular channel for the transfer of lipid radicals from mitochondria to the ER for clearance

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Extracts were processed exactly as described in Cellular metabolomics analysis, including homogenization, protein precipitation, sonication, vacuum concentration, and HILIC reconstitution

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The breakdown of GSH (and also of its oxidized form, GSSG) is catalyzed by -glutamyl transpeptidase, which catalyzes the transfer of the gamma-glutamyl moiety to acceptors such as SH-containing amino acids, certain dipeptides, and GSH itself (Reaction 3)