Figure 2
From: Palmitoylation: a protein S-acylation with implications for breast cancer
(a) The ability of ESR1 and ESR2 to associate with scaffolding and/or signaling proteins at the plasma membrane is principally due to palmitoylation. Mutation of ESR1 Cys447 to Ala prevents palmitoylation, plasma membrane localization, association with caveolin-1 (CAV1), and non-genomic activities.56 Palmitoylation of ESR2 was established in a human colon adenocarcinoma cell line, which contains only one ESR2 isoform.61 ESR2 association with caveolin-1 and p38 was prevented by pretreatment with the protein acyltransferases (PAT) inhibitor 2-bromohexadecanoic acid. (b) E2-induced membrane-associated ER36 mediates anti-apoptotic effect in triple-negative breast cancer cells. Palmitoylated ER36 translocates to the plasma membrane and enacts two independent pathways: PI3K signaling that requires interaction with phosphatidylcholine-specific phospholipase D (PC-PLD) and lysophosphatidic acid (LPA), and ERK1/2 signaling involving phosphatidylinositol-specific phospholipase C (PI-PLC) and protein kinase C (PKC).62
