Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction.
Am J Physiol
; 268(3 Pt 1): C563-71, 1995 Mar.
Article
en En
| MEDLINE
| ID: mdl-7534979
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.
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Base de datos:
MEDLINE
Asunto principal:
Fosfoproteínas
/
Tráquea
/
Talina
/
Proteínas del Citoesqueleto
/
Contracción Muscular
Límite:
Animals
Idioma:
En
Revista:
Am J Physiol
Año:
1995
Tipo del documento:
Article