Palmitoylation of caveolin-1 is regulated by the same DHHC acyltransferases that modify steroid hormone receptors

The Journal of Biological Chemistry
Katherine R Tonn EisingerP G Mermelstein

Abstract

Palmitoylation is a reversible post-translational addition of a 16-carbon lipid chain involved in trafficking and compartmentalizing target proteins. It is important for many cellular functions, including signaling via membrane-localized estrogen receptors (ERs). Within the nervous system, palmitoylation of ERα is necessary for membrane surface localization and mediation of downstream signaling through the activation of metabotropic glutamate receptors (mGluRs). Substitution of the single palmitoylation site on ERα prevents its physical association with the integral membrane protein caveolin-1 (CAV1), required for the formation of the ER/mGluR signaling complex. Interestingly, siRNA knockdown of either of two palmitoyl acyltransferases, zinc finger DHHC type-containing 7 (DHHC7) or DHHC21, also eliminates this signaling mechanism. Because ERα has only one palmitoylation site, we hypothesized that one of these DHHCs palmitoylates CAV1. We investigated this possibility by using an acyl-biotin exchange assay in HEK293 cells in conjunction with DHHC overexpression and found that DHHC7 increases CAV1 palmitoylation. Substitution of the palmitoylation sites on CAV1 eliminated this effect but did not disrupt the ability of the DHHC en...Continue Reading

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Citations

Feb 29, 2020·International Journal of Molecular Sciences·Manuel Alvarez-RodriguezHeriberto Rodriguez-Martinez
May 21, 2020·Journal of Neurophysiology·Stephanie B Proaño, John Meitzen
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Nov 6, 2021·Biology of the Cell·Maxime Jansen, Bruno Beaumelle

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