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J. Biol. Chem., Vol. 276, Issue 2, 993-998, January 12, 2001
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From the Instituto de Investigaciones Citológicas, 46010 Valencia, Spain
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-
The Tumor Suppressor PTEN Is Phosphorylated by the Protein
Kinase CK2 at Its C Terminus
IMPLICATIONS FOR PTEN STABILITY TO PROTEASOME-MEDIATED
DEGRADATION*
and
-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.
*
This work was supported by grants from the Ministerio de
Educación y Cultura (PB96-0278) and the Generalitat Valenciana
(GV-C-VS-20-047-96).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a fellowship from Generalitat Valenciana.
§
To whom correspondence should be addressed: Instituto de
Investigaciones Citológicas, c/Amadeo de Saboya 4, 46010, Valencia, Spain. Tel.: 96-3391256; Fax: 96-3601453; E-mail:
rpulido@ochoa.fib.es.
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