DAPK功能機制與訊息網路之研究(1/5)
Date Issued
2005-05-26
Date
2005-05-26
Author(s)
Chen, Ruey-Hwa
DOI
932321B002017
Abstract
Death-associated protein kinase (DAPK) is a death domain-containing serine/threonine
kinase, and participates in various apoptotic paradigms. Here, we identify the extracellular
signal-regulated kinase (ERK) as a DAPK-interacting protein. DAPK interacts with ERK
through a docking sequence within its death domain and is a substrate of ERK.
Phosphorylation of DAPK at Ser 735 by ERK increases the catalytic activity of DAPK both
in vitro and in vivo. Conversely, DAPK promotes the cytoplasmic retention of ERK,
thereby inhibiting ERK signaling in the nucleus. This reciprocal regulation between DAPK
and ERK constitutes a positive feedback loop that ultimately promotes the apoptotic activity
of DAPK. In a physiological apoptosis system where ERK-DAPK interplay is reinforced,
downregulation of either ERK or DAPK suppresses such apoptosis. These results indicate
that bi-directional signalings between DAPK and ERK may contribute to the
apoptosis-promoting function of the death domain of DAPK.
Subjects
anoikis
DAPK
death domain/ERK
Publisher
臺北市：國立臺灣大學醫學院分子醫學研究所
Type
journal article
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