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J. Biol. Chem., Vol. 275, Issue 28, 21477-21485, July 14, 2000
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From the Departments of Molecular Oncology and
PTEN/MMAC is a phosphatase that is mutated in
multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated
phosphatidylinositol phosphates that activate AKT/protein kinase B
(PKB) kinase activity. AKT/PKB is implicated in the inhibition of
apoptosis, and cell lines and tumors with mutated PTEN/MMAC show
increased AKT/PKB kinase activity and resistance to apoptosis.
PTEN/MMAC contains a PDZ domain-binding site, and we show here that the
phosphatase binds to a PDZ domain of
membrane-associated guanylate
kinase with inverted orientation (MAGI) 3, a novel inverted
membrane-associated guanylate kinase that localizes to epithelial cell
tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate
the kinase activity of AKT/PKB. These data suggest that MAGI3 allows
for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) 331900.
Interaction of the Tumor Suppressor PTEN/MMAC with a PDZ Domain
of MAGI3, a Novel Membrane-associated Guanylate Kinase*
,, and Molecular Biology, Genentech, Inc.,
South San Francisco, California 94080
*
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.
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