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

Fredrick Pavalko, L. P. Adam, M. F. Wu, T. L. Walker, Susan Gunst

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

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
JournalAmerican Journal of Physiology - Cell Physiology
Volume268
Issue number3 37-3
StatePublished - 1995

Fingerprint

talin
Talin
Paxillin
Phosphorylation
muscle contraction
Muscle Contraction
smooth muscle
Smooth Muscle
Muscle
phosphorylation
Vinculin
Proteins
proteins
Membranes
threonine
serine
tyrosine
phosphotransferases (kinases)
Phosphopeptides
Protein-Serine-Threonine Kinases

Keywords

  • acetylcholine
  • cytoskeleton
  • immunoprecipitation
  • phosphotyrosine

ASJC Scopus subject areas

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

Cite this

Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction. / Pavalko, Fredrick; Adam, L. P.; Wu, M. F.; Walker, T. L.; Gunst, Susan.

In: American Journal of Physiology - Cell Physiology, Vol. 268, No. 3 37-3, 1995.

Research output: Contribution to journalArticle

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AU - Adam, L. P.

AU - Wu, M. F.

AU - Walker, T. L.

AU - Gunst, Susan

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N2 - 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.

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