Thousands of proteins have been found to be modified by O-GlcNAc, a common type of glycosylation on serine and threonine residues throughout the cytosol and nucleus. However, compared to other posttranslational modifications, relatively few O-GlcNAc regulated pathways have been discovered and biochemically characterized. We previously discovered one such pathway, where O-GlcNAc controls the contraction of fibroblasts initiated by the signaling lipid sphingosine-1-phosphate. Here, we demonstrate that these same O-GlcNAc modifications on the phosphatase MYPT1 also control the sensitivity of fibroblasts to contraction signaling mediated by lysophosphatidic acid.

O-GlcNAc modification of MYPT1 controls the sensitivity of fibroblast signaling for contraction

ACS Spring 2022

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