Journal
TRENDS IN ENDOCRINOLOGY AND METABOLISM
Volume 19, Issue 6, Pages 223-230Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tem.2008.04.001
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Funding
- National Institutes of Health [R01 GM43154, GM067946]
- Department of Defense Breast Cancer Research Program Predoctoral [BC043239]
- U.S. Army Medical Research Acquisition Activity
- Fort Detrick [MD21702-5014]
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The Ser/Thr-specific phosphatase PHLPP pleckstrin homology (PH) domain leucine-rich repeat protein phosphatasel provides 'the brakes' for Akt and protein kinase C (PKC) signaling. The two isoforms of this recently discovered family, PHLPP1 and PHLPP2, control the amplitude and duration of signaling of Akt and PKC by catalyzing the dephosphorylation of the hydrophobic phosphorylation motif, a C-terminal phosphorylation switch that controls these kinases. Aberrant regulation of either kinase accompanies many diseases, notably diabetes and cancer. By specifically dephosphorylating the hydrophobic motif, PHLPP controls the degree of agonist-evoked signaling by Akt and the cellular levels of PKC. This review focuses on the function of PHLPP1 and PHLPP2 in modulating signaling by Akt and PKC.
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