The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
The Tumor Suppressor PTEN Is Phosphorylated by the Protein Kinase CK2 at Its C Terminus
Open accessAbstract
The tumor suppressor phosphatase PTEN regulates cell migration, growth, and survival by dephosphorylating phosphatidylinositol second messengers and signaling phosphoproteins. PTEN possesses a C-terminal noncatalytic regulatory domain that contains multiple putative phosphorylation sites, which could play an important role in the control of its biological activity. The protein kinase CK2 phosphorylated, in a constitutive manner, a cluster of Ser/Thr residues located at the PTEN C terminus. PTEN-phosphorylated defective mutants showed decreased stability in comparison with wild type PTEN and were more rapidly degraded by the proteasome. Inhibition of PTEN phosphorylation by the CK2 inhibitor 5,6-dichloro-1-beta-d-ribofuranosyl-benzimidazole also diminished the PTEN protein content. Our results support the notion that proper phosphorylation of PTEN by CK2 is important for PTEN protein stability to proteasome-mediated degradation.
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One‐thousand‐and‐one substrates of protein kinase CK2?
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NEDD4-1 Is a Proto-Oncogenic Ubiquitin Ligase for PTEN
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Modulation of mammalian life span by the short isoform of p53
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Metadata
- Authors
- Torres, J., & Pulido, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 276
- Issue
- 2
- Pages
- 993-998
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1988769784
- Cited by
- 629
- References
- 47
- FWCI
- 8.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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