O-GlcNAcylation is a posttranslational modification (PTM) involving the addition of the carbohydrate N-acetyl-glucosamine (O-GlcNAc) to serine and threonine side chains of intracellular proteins. Two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), facilitate the addition and removal of O-GlcNAc respectively. The levels of O-GlcNAcylation are directly involved in maintaining homeostasis in cells. Misregulation has been linked to a range of diseases including cancer and neurodegeneration. However, a complete understanding of which proteins are O-GlcNAc modified and the role this PTM plays in stabilizing and sustaining cells has not been fully clarified. Recently, it was observed that inhibiting OGT, functionally preventing O-GlcNAcylation, before treatment with sphingosine-1-phosphate (S1P) leads to a contraction phenotype in fibroblast cells. Here, we first investigate key proteins implicated in S1P signaling. Results of these experiments demonstrate that the modification of myosin phosphate target subunit 1 (MYPT1) controls that phosphorylation status of myosin to regulate the relaxation versus contraction status of fibroblast cells.

O-GlcNAcylation of myosin phosphatase target subunit 1 controls the sensitivity of sphingosine-1-phosphate signaling in fibroblasts

2019 Fall National Meeting

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