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J Biol Chem, Vol. 274, Issue 19, 13085-13090, May 7, 1999
,,, and
From the With the amino acid sequences of all reported Akt
kinase physiological substrates, the possible Akt kinase substrate
specificity has been suggested. The serine/threonine residue to be
phosphorylated in these proteins is placed within stretches of amino
acids with homology, and the arginine residues on the Shin Dong Bang R&D Center,
5 and 3
positions and a hydrophobic amino acid on the +2 position are conserved relative to those of serine/threonine residues
(XXRXRXXS/TXX). We
noticed two putative Akt kinase phosphorylation sites
(220GARRRGGSAS229)
and
(817AVRIRGKSYV826)
in human telomerase reverse transcriptase (hTERT) subunit. To demonstrate that hTERT is an Akt kinase substrate protein, we performed
the nonradioactive protein kinase assay with the fluorescein hTERT
peptide
(817AVRIRGKSYV826).
We observed the phosphorylation of hTERT peptide by the human melanoma
cell lysate or the activated recombinant Akt kinase proteins in
vitro. With the treatment of the growth factor deprivation or
okadaic acid, we also observed the up-regulation of both hTERT peptide
phosphorylation and the telomerase activity. We noticed that Wortmannin
down-regulates hTERT peptide phosphorylation and telomerase activity
together. In addition, we observed the enhancement of telomerase
activity with the pretreatment of Akt kinase in vitro.
Thus, these observations suggest that Akt kinase enhances human
telomerase activity through phosphorylation of hTERT subunit as one of
its substrate proteins.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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