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J. Biol. Chem., Vol. 276, Issue 22, 19102-19110, June 1, 2001
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From the AMP-activated protein kinase (AMPK) is tightly
regulated by the cellular AMP:ATP ratio and plays a central role in the
regulation of energy homeostasis. Previously, AMPK was reported to
phosphorylate serine 621 of Raf-1 in vitro. In the present
study, we investigated a possible role of AMPK in extracellular
signal-regulated kinase (Erk) cascades, using
5-aminoimidazole-4-carboxamide-1-
Effects of Stimulation of AMP-activated Protein Kinase on
Insulin-like Growth Factor 1- and Epidermal Growth
Factor-dependent Extracellular Signal-regulated Kinase
Pathway*
,,
Department of Chemistry, Hanyang University,
Seoul 133-791, Korea and the § Department of Molecular
Biology, East-West Medical Research Center and the ¶ Department of
Internal Medicine, Kyung Hee University, College of Medicine,
Seoul 130-701, Korea
-D-ribofuranoside (AICAR), a cell-permeable activator of AMPK and antisense RNA experiments. Activation of AMPK by AICAR in NIH-3T3 cells resulted in
drastic inhibitions of Ras, Raf-1, and Erk activation induced by
insulin-like growth factor 1 (IGF-1). Expression of an antisense RNA
for the AMPK catalytic subunit decreased the AMPK activity and
significantly diminished the AICAR effect on IGF-1-induced Ras
activation and the subsequent Erk activation, indicating that its
effect is indeed mediated by AMPK. Phosphorylation of Raf-1 serine 621, however, was not involved in AMPK-mediated inhibition of Erk cascades.
In contrast to IGF-1, AICAR did not block epidermal growth factor
(EGF)-dependent Raf-1 and Erk activation, but our results
demonstrated that multiple Raf-1 upstream pathways induced by EGF were
differentially affected by AICAR: inhibition of Ras activation and
simultaneous induction of Ras-independent Raf activation. The
activities of IGF-1 and EGF receptor were not affected by AICAR. Taken
together, our results suggest that AMPK differentially regulate Erk
cascades by inhibiting Ras activation or stimulating the
Ras-independent pathway in response to the varying energy status of the cell.
*
This work was supported by Korea Research Foundation Grant
KRF-99-041-F00012 and Ministry of Health and Welfare Grant
HMP-98-B-2-0011.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Molecular Biology, East-West Medical Research Center, Kyung Hee
University College of Medicine, Tongdaemun-gu, Hoegi-dong 1, Seoul
130-701, Korea. Tel.: 82-2-961-0921; Fax: 82-2-959-8168; E-mail:
hajh@khu.ac.kr.
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