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in muscle cells of the colon
Department of Pediatrics, University of Michigan Medical Center, Ann Arbor, Michigan 48109
The recruitment of signal
transduction molecules to the membrane is crucial for the efficient
coupling of extracellular signals and contractile response. The
trafficking is dynamic. We have investigated a possible cross talk
between agonist-induced association of translocated RhoA and
translocated protein kinase C-
(PKC-) and a role for heat shock
protein 27 (HSP27) in mediating this interaction. Immunoprecipitation
with HSP27 monoclonal antibody followed by immunoblotting with either
RhoA antibody or PKC- antibody indicated that acetylcholine induced
associations of HSP27-RhoA and HSP27-PKC- in the membrane fraction
but not in the cytosolic fraction. Immunoprecipitation with
anti-RhoA monoclonal antibody followed by immunoblotting with PKC-
antibody indicated that acetylcholine induced a significant complexing
of RhoA-PKC- in the membrane fraction but not in the cytosolic
fraction. In summary, the data indicate that agonist-induced
contraction is associated with 1) association of
translocated RhoA with HSP27 on the membrane, 2) association
of translocated PKC- with HSP27 on the membrane, and 3)
association of PKC- with RhoA on the membrane. The data suggest an
important role for HSP27 in modulating a multiprotein complex that
includes translocated RhoA and PKC-.
cytoskeleton; contraction; signal transduction; heat shock protein
27; protein kinase C-
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