PTEN, or phosphatase and tensin homolog, is a tumor suppressor protein that plays a crucial role in regulating cell growth, survival, and migration by antagonizing the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway. Phosphorylation of PTEN is an important post-translational modification that can affect its stability, subcellular localization, and enzymatic activity. The phosphorylation at S380, along with other residues such as T382 and T383, has been shown to be critical for the regulation of PTEN's function. Phosphorylation at these sites can lead to decreased stability of the PTEN protein, which in turn can affect its ability to suppress tumorigenesis. This post-translational modification can also influence the interaction of PTEN with other cellular proteins, impacting its downstream signaling effects. In the context of cancer, the phosphorylation state of PTEN is closely monitored as it can serve as a potential biomarker for prognosis and therapeutic response. Dysregulation of PTEN phosphorylation, including the S380 site, has been implicated in various cancers, suggesting its importance in tumor development and progression.
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