DAPK2 or death-associated protein kinase 2 belongs to a family of proapoptotic Ca(2+)/calmodulin-regulated serine/threonine kinases. Overexpression of DAPK2 induces cell apoptosis. DAPK2 has been shown to be a novel Sp1-dependent target gene for E2F1 and Krüppel-like factor 6 (KLF6) in cell death response. Both E2F1 and KLF6 strongly activate the DAPK2 promoter. DAPK2 plays a role in granulopoiesis where it is highly expressed. β-catenin can block anoikis of malignant kidney and intestinal epithelial cells and promote their anchorage-independent growth by down-regulating DAPK2. β-catenin-induced down-regulation of DAPK2 requires the presence of the transcription factor TCF-4.
Death-associated protein kinase 2 (DAPK2) belongs to a family of proapoptotic Ca(2+)/calmodulin-regulated serine/threonine kinases. We recently identified DAPK2 as an enhancing factor during granulocytic differentiation. To identify transcriptional DAPK2 regulators, we cloned 2.7 kb of the 5'-flanking region of the
The Journal of biological chemistry, 284(4), 2012-2022 (2008-10-30)
Resistance of solid tumor cells to anoikis, apoptosis induced by cell detachment from the extracellular matrix, is thought to be critical for the ability of these cells to grow anchorage independently within three-dimensional tumor masses and from metastases. Beta-catenin, a
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