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

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,

SUBMITTER: Tonn Eisinger KR 

PROVIDER: S-EPMC6187622 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature