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O‐GlcNAcylation regulates lysophosphatidic acid‐induced cell migration by regulating ERM family proteins

O‐GlcNAcylation of intracellular proteins (O‐GlcNAc) is a post‐translational modification that often competes with phosphorylation in diverse cellular signaling pathways. Recent studies on human malignant tumors have demonstrated that O‐GlcNAc is implicated in cellular features relevant to metastasi...

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Detalles Bibliográficos
Autores principales: Song, Minseok, Suh, Pann‐Ghill
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9157403/
https://www.ncbi.nlm.nih.gov/pubmed/35347892
http://dx.doi.org/10.1002/2211-5463.13404
Descripción
Sumario:O‐GlcNAcylation of intracellular proteins (O‐GlcNAc) is a post‐translational modification that often competes with phosphorylation in diverse cellular signaling pathways. Recent studies on human malignant tumors have demonstrated that O‐GlcNAc is implicated in cellular features relevant to metastasis. Here, we report that lysophosphatidic acid (LPA)‐induced ovarian cancer cell (OVCAR‐3) migration is regulated by O‐GlcNAc. We found that O‐GlcNAc modification of ERM family proteins, a membrane‐cytoskeletal crosslinker, was inversely correlated with its phosphorylation status. Moreover, the LPA‐induced formation of membrane protrusion structures, as well as the migration of OVCAR‐3 cells, was reduced by the accumulation of O‐GlcNAc. Collectively, these findings suggest that O‐GlcNAc is an essential signaling element controlling ERM family proteins involved in OVCAR‐3 cell migration.