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J Biol Chem, Vol. 273, Issue 33, 21099-21104, August 14, 1998
From the Department of Cell Biology and Neuroscience, University of
Texas Southwestern Medical Center, Dallas, Texas 75235
Previously we showed that activation of Erk in
quiescent cells occurs in the caveolae fraction isolated from
fibroblasts. Since the structure and function of caveolae is sensitive
to the amount of cholesterol in the membrane, it might be that a direct link exists between the concentration of membrane cholesterol and
mitogen-activated protein (MAP) kinase activation. We acutely lowered
the cholesterol level of the caveolae fraction by incubating Rat-1
cells in the presence of either cyclodextrin or progesterone. Cholesterol-depleted caveolae had a reduced amount of several key
protein components of the MAP kinase complex, including Ras, Grb2,
Erk2, and Src. Incubation of these cells in the presence of epidermal
growth factor (EGF) caused a rapid loss of EGF receptor from the
caveolae fraction, but the usual recruitment of c-Raf was markedly
inhibited. Despite the reduced amount of c-Raf and Erk2 in the
cholesterol-depleted caveolae fraction, EGF caused a hyperactivation of
the remaining caveolae Erk isoenzymes. This was followed by an increase
in the amount of active Erk in the cytoplasm. The increased amount of
activated Erk produced under these conditions was linked to a 2-fold
higher level of EGF-stimulated DNA synthesis. Even cholesterol
depletion by itself stimulated Erk activation and DNA synthesis. These
results suggest that the MAP kinase pathway can connect the cholesterol
level of caveolae membrane to the control of cell division.
Cholesterol Depletion of Caveolae Causes Hyperactivation of
Extracellular Signal-related Kinase (ERK)
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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