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Updated: Jun 10, 2025

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
S-acylation of Ca2+ transport proteins in cancer
Sana Kouba1, Nicolas Demaurex1
1Department of Cell Physiology and Metabolism Centre Médical Universitaire, University of Geneva Geneva Switzerland.
Abstract:
Alterations in cellular calcium (Ca2+) signals have been causally associated with the development and progression of human cancers. Cellular Ca2+ signals are generated by channels, pumps, and exchangers that move Ca2+ ions across membranes and are decoded by effector proteins in the cytosol or in organelles. S-acylation, the reversible addition of 16-carbon fatty acids to proteins, modulates the activity of Ca2+ transporters by altering their affinity for lipids, and enzymes mediating this reversible post-translational modification have also been linked to several types of cancers. Here, we compile studies reporting an association between Ca2+ transporters or S-acylation enzymes with specific cancers, as well as studies reporting or predicting the S-acylation of Ca2+ transporters. We then discuss the potential role of S-acylation in the oncogenic potential of a subset of Ca2+ transport proteins involved in cancer.
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