Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction

F. M. Pavalko, L. P. Adam, M. F. Wu, T. L. Walker, S. J. Gunst

Research output: Contribution to journalArticlepeer-review

72 Scopus citations


Reorganization of cytoskeletal-membrane interactions during contractile stimulation may contribute to the regulation of airway smooth muscle contraction. We investigated the effect of contractile stimulation on the phosphorylation of the actin-membrane attachment proteins talin, vinculin, and paxillin. Stimulation of 32P-labeled canine tracheal smooth muscle strips with acetylcholine (ACh; 10-3 M) resulted in a rapid 2.6-fold increase in phosphorylation of serine and/or threonine residues, compared with resting levels of 0.22 mol PO4/3-/mol talin. After stimulation with ACh, phosphorylation of tyrosine residues on paxillin increased approximately threefold. Two-dimensional phosphopeptide mapping of in vivo labeled talin and paxillin indicated phosphorylation on a limited number of sites. Vinculin phosphorylation was undetectable in either resting or ACh-stimulated muscle. We conclude that phosphorylation of talin and paxillin occurs during ACh- stimulated contraction of tracheal smooth muscle and that distinct signaling pathways activate a serine/threonine kinase that phosphorylates talin and a tyrosine kinase that phosphorylates paxillin. The pharmacological activation of airway smooth muscle cells might involve the anchoring of contractile filaments to the membrane.

Original languageEnglish (US)
Pages (from-to)C563-C571
JournalAmerican Journal of Physiology - Cell Physiology
Issue number3 37-3
StatePublished - 1995


  • acetylcholine
  • cytoskeleton
  • immunoprecipitation
  • phosphotyrosine

ASJC Scopus subject areas

  • Cell Biology
  • Clinical Biochemistry
  • Physiology
  • Agricultural and Biological Sciences(all)

Fingerprint Dive into the research topics of 'Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction'. Together they form a unique fingerprint.

Cite this