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(Received for publication, May 22, 1997, and in revised form, July 29, 1997)
From the Contraction of smooth muscle cells is generally
assumed to require
Ca2+/calmodulin-dependent phosphorylation
of the 20-kDa myosin light chains. However, we report here that in the
absence of extracellular calcium, phenylephrine induces a contraction
of freshly isolated ferret aorta cells in the absence of increases in
intracellular ionized calcium or light chain phosphorylation
levels but in the presence of activation of mitogen-activated
protein kinase. A protein at 36 kDa co-immunoprecipitated with the
mitogen-activated protein kinase and was identified as the
actin-binding protein, calponin, by immunoblot. An overlay assay
further confirmed an interaction between the kinase and calponin, even
though the kinase did not phosphorylate calponin in vitro.
Calponin also co-immunoprecipitated from smooth muscle cells with
protein kinase C-
Volume 272, Number 40,
Issue of October 3, 1997
pp. 25157-25161
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,§
,
and§
Signal Transduction Group, Boston Biomedical
Research Institute, Boston, Massachusetts 02114 and the
§ Cardiovascular Division, Beth Israel Deaconess Medical
Center, and Harvard Medical School, Boston, Massachusetts 02215
. High resolution digital confocal studies
indicated that calponin redistributes to the cell membrane during
phenylephrine stimulation at a time when mitogen-activated protein
kinase and protein kinase C- are targeted to the plasmalemma. These
results suggest a role for calponin as a signaling molecule, possibly
an adapter protein, linking the targeting of mitogen-activated protein
kinase and protein kinase C- to the surface membrane.
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