cGMP-dependent protein kinase I promotes cell apoptosis through hyperactivation of death-associated protein kinase 2

Biochemical and Biophysical Research Communications
Kinuka IsshikiKeizo Yuasa

Abstract

cGMP-dependent protein kinase-I (cGK-I) induces apoptosis in various cancer cell lines. However, the signaling mechanisms involved remain unknown. Using protein microarray technology, we identified a novel cGK substrate, death-associated protein kinase 2 (DAPK2), which is a Ca(2+)/calmodulin-regulated serine/threonine kinase. cGK-I phosphorylated DAPK2 at Ser(299), Ser(367) and Ser(368). Interestingly, a phospho-mimic mutant, DAPK2 S299D, significantly enhanced its kinase activity in the absence of Ca(2+)/calmodulin, while a S367D/S368D mutant did not. Overexpression of DAPK2 S299D also resulted in a twofold increase in apoptosis of human breast cancer MCF-7 cells as compared with wild-type DAPK2. These results suggest that DAPK2 is one of the targets of cGK-I in apoptosis induction.

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Citations

Nov 4, 2015·Biochemical and Biophysical Research Communications·Kinuka IsshikiKeizo Yuasa
Jun 7, 2015·Biochemical and Biophysical Research Communications·Keizo YuasaAkihiko Tsuji
Jun 10, 2015·The International Journal of Biochemistry & Cell Biology·Barbara Geering
Jun 28, 2014·Seminars in Cancer Biology·Perrin F Windham, Heather N Tinsley
Jul 5, 2013·American Journal of Physiology. Renal Physiology·Hasiyeti MaimaitiyimingShuxia Wang
Oct 6, 2018·International Journal of Molecular Sciences·Mohamed ElbadawyKazuaki Sasaki

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