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Am J Physiol Cell Physiol 274: C741-C747, 1998;
0363-6143/98 $5.00
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Vol. 274, Issue 3, C741-C747, March 1998

Relationship between paxillin and myosin phosphorylation during muscarinic stimulation of smooth muscle

Dolly Mehta, Zhonglin Wang, Ming-Fang Wu, and Susan J. Gunst

Department of Physiology and Biophysics, Indiana University School of Medicine, Indianapolis, Indiana 46202

The tyrosine phosphorylation of paxillin increases in association with force development during tracheal smooth muscle contraction, suggesting that paxillin plays a role in the contractile activation of smooth muscle [Z. L. Wang, F. M. Pavalko, and S. J. Gunst. Am. J. Physiol. 271 (Cell Physiol. 40): C1594-C1602, 1996]. We compared the Ca2+ sensitivity of the tyrosine phosphorylation of paxillin and myosin light chain (MLC) phosphorylation in tracheal muscle and evaluated whether MLC phosphorylation is necessary to induce paxillin phosphorylation. Ca2+-depleted muscle strips were stimulated with 10-7-10-4 M acetylcholine (ACh) in 0, 0.05, 0.1, or 0.5 mM extracellular Ca2+. In the absence of extracellular Ca2+, 10-4 M ACh induced a maximal increase in paxillin phosphorylation without increasing MLC phosphorylation or force. Increases in extracellular Ca2+ concentration did not further increase paxillin phosphorylation. However, during stimulation with 10-6 M ACh, paxillin phosphorylation increased with increases in extracellular Ca2+ concentration. We conclude that the tyrosine phosphorylation of paxillin can be stimulated by signaling pathways that do not depend on Ca2+ mobilization and that the activation of contractile proteins is not required to elicit paxillin phosphorylation.

myosin light chain phosphorylation; cytoskeleton; focal adhesion proteins; smooth muscle contraction


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