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J. Biol. Chem., Vol. 281, Issue 36, 99929, September 8, 2006

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PTEN Regulation by Acetylation

PTEN is an important tumor suppressor in human cancer that also plays a role in the regulation of cell migration, growth, and apoptosis. These functions are mediated by the protein's lipid phosphatase activity, which inhibits the phosphatidylinositol 3-kinase (PI3K) signaling pathway. Despite this protein's crucial role in many biological processes, the mechanisms governing PTEN activity remain unclear.

PTEN and PCAF co-localize in cells.

This Paper of the Week establishes that PTEN lipid phosphatase activity is inhibited when the protein is acetylated by the histone acetyltransferase PCAF (p300/CBP-associated factor). Koichi Okumura and colleagues show that expression of PCAF results in increased acetylation of two lysine residues within the catalytic cleft of PTEN, a structure essential for PI3K specificity. Furthermore, reduction of endogenous PCAF activity using short hairpin RNA (shRNA) results in a loss of PTEN acetylation and restores the ability of PTEN to downregulate PI3K signaling and to induce G₁ cell cycle arrest. The authors also demonstrate that acetylation-resistant PTEN mutants are able to retain their PI3K signaling in the presence of PCAF. These results emphasize the importance of protein acetylation in biochemical pathways and provide further insight into the role of PTEN in the development of human diseases.

FOOTNOTES

See referenced article, J. Biol. Chem. 2006, 281, 26562-26568

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Related Collections Papers Of The Week Social Bookmarking                      What's this?