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Am J Physiol Cell Physiol (February 9, 2005). doi:10.1152/ajpcell.00399.2004
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Submitted on August 15, 2004
Accepted on February 8, 2005

Maxi-K channels Localize to Caveolae in Human Myometrium: A Role for an Actin-Channel-Caveolin complex in the Regulation of Myometrial Smooth Muscle K+ Current

Adam M. Brainard1, Andrea J. Miller1, Jeffrey R. Martens1, and S.K. England1*

1 Department of Physiology and Biophysics, University of Iowa Carver College of Medicine, Iowa City, Iowa, USA

* To whom correspondence should be addressed. E-mail: sarah-england{at}uiowa.edu.

Multiple cell-signaling pathways converge to modulate maxi-K channel activity and buffer cell excitability in human myometrial smooth muscle cells (hMSMCs). Recent evidence indicates that maxi-K channel proteins can target to membrane microdomains; however, their associations with other proteins within these macromolecular complexes has not been elucidated. Biochemical isolation of detergent-resistant membrane fractions from human myometrium demonstrates the presence of maxi-K channels in lipid raft microdomains, which co-fractionate with caveolins. In both non-pregnant and late-pregnant myometrium, maxi-K channels associate and co-localize with caveolar scaffolding proteins caveolin-1 and -2, but not caveolin-3. Disruption of cultured hMSMC caveolar complexes by cholesterol depletion with cyclodextrin increases an iberiotoxin-sensitive K+ current. Co-immunoprecipitations indicate that the maxi-K channel is also associated with both {alpha}- and {gamma}-actin. Immunocytochemical analysis indicates colocalization of maxi-K channels, actin, and caveolin-1 in primary cultures of hMSMCs. Further experiments using immunoelectron microscopy illustrate the proximity of both actin and the maxi-K channel within the same cell-surface caveolar structures. Functionally, disruption of the actin cytoskeleton in cultured hMSMCs by cytochalasin D and latrunculin A greatly increased the open-state probability of the channel, while stabilization of actin cytoskeleton with jasplakinolide abolished the effect of latrunculin A. These data indicate that the actin cytoskeleton, as part of a caveolar complex, is involved in the regulation of myometrial maxi-K channel function.




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