Phosphorylation of the PTEN Tail Regulates Protein Stability and Function

By F. Vazquez, Shivapriya Ramaswamy, N. Nakamura, William R. Sellers. Molecular and Cellular Biology, 2000

812 citations recorded by the source corpus.

Subfields: Molecular Biology, Pathology and Forensic Medicine

View Paper: https://www.semanticscholar.org/paper/342e0e012e6b90f54f4424d128792b744628cedf

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In Molecular Biology

In Pathology and Forensic Medicine

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Citations in the corpus

Tenets of PTEN tumor suppression. (2008, background): “…2008 ©2008 Elsevier Inc. rylation of PTEN at specific residues in its C-terminal tail have been associated with increased stability (Georgescu et al., 1999; Torres and Pulido, 2001; Vazquez et al., 2000), whereas phosphorylation at other sites may decrease protein stability (Maccario et al., 2007).”
NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. (2007, positive): “PTEN has been shown to be phosphorylated in cells, and the phosphorylation appears to affect PTEN function (Adey et al., 2000; Leslie and Downes, 2004; Torres and Pulido, 2001; Vazquez et al., 2000).”
Multiplex Assessment of Protein Variant Abundance by Massively Parallel Sequencing (2018, background): “Active site or C-terminal regulatory phosphosite variants have been found to decrease activity, reduce membrane binding and increase abundance, hinting at the existence of a negative feedback mechanism that degrades membrane-bound, active PTEN 31,32 .”
A saturation mutagenesis approach to understanding PTEN lipid phosphatase activity and genotype-phenotypes relationships (2018, background): “Additionally, an intramolecular regulatory interaction between the C-terminal tail and the phosphatase domain is controlled by phosphorylation at four sites in the tail, in mammalian cells.(51) We find that individual phosphomimetic substitutions at these sites are insufficient to decrease activity ”
Akt/protein kinase B is constitutively active in non-small cell lung cancer cells and promotes cellular survival and resistance to chemotherapy and radiation. (2001, background): “Of note, PTEN regulation of Akt/PKB is complicated further by the demonstration that PTEN function is regulated by phosphorylation (79).”
Malignant glioma: genetics and biology of a grave matter. (2001, background): “Furthermore, although some mutants of PTEN that lack growth-suppressive activity are invariably defective for 3’ phosphoinositol phosphatase activity, some retain activity against protein substrates (Furnari et al. 1998; Myers et al. 1998; Vazquez et al. 2000), indicating that the lipid phosphatase ”
Dysregulation of AKT Pathway by SMYD2-Mediated Lysine Methylation on PTEN (2015, neutral): “This phosphorylation was reported to be involved in inactivation of PTEN tumor suppressor functions by promoting “closed conformation” of PTEN and resulting in dissociation of the C2 domain from the membrane [15,35].”
PTEN: One Gene, Many Syndromes (2003, background): “The Cterminal domain also contains the PEST domains (amino acids 350–375 and 379–396), which regulate protein stability, and the PDZ domain, important in protein– protein interactions [Georgescu et al., 1999; Lee et al., 1999; Vazquez et al., 2000].”