O-GlcNAc modification of MYPT1 modulates lysophosphatidic acid-induced cell contraction in fibroblasts.

ABSTRACT: Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus. O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling. However, compared with other posttranslational modifications like phosphorylation, 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. Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of

SUBMITTER: Morales MM 

PROVIDER: S-EPMC8191289 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature