Vasodilator-stimulated phosphoprotein (VASP) regulates actin polymerization and contraction in airway smooth muscle by a vinculin-dependent mechanism

Yidi Wu, Susan Gunst

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Background: The function of vasodilator-stimulated phosphoprotein (VASP) in regulating actin polymerization during airway smooth muscle contraction is unknown. Results: VASP activity requires phosphorylation at Ser157, recruitment to the membrane, and interaction with activated vinculin. Conclusion: VASP regulates actin polymerization and contraction in smooth muscle by a unique mechanism. Significance: The mechanism of VASP function is important for understanding actin dynamics in cells.

Original languageEnglish
Pages (from-to)11403-11416
Number of pages14
JournalJournal of Biological Chemistry
Volume290
Issue number18
DOIs
StatePublished - May 1 2015

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Vinculin
Polymerization
Smooth Muscle
Muscle
Actins
Phosphorylation
Muscle Contraction
Membranes
vasodilator-stimulated phosphoprotein

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

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title = "Vasodilator-stimulated phosphoprotein (VASP) regulates actin polymerization and contraction in airway smooth muscle by a vinculin-dependent mechanism",
abstract = "Background: The function of vasodilator-stimulated phosphoprotein (VASP) in regulating actin polymerization during airway smooth muscle contraction is unknown. Results: VASP activity requires phosphorylation at Ser157, recruitment to the membrane, and interaction with activated vinculin. Conclusion: VASP regulates actin polymerization and contraction in smooth muscle by a unique mechanism. Significance: The mechanism of VASP function is important for understanding actin dynamics in cells.",
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N2 - Background: The function of vasodilator-stimulated phosphoprotein (VASP) in regulating actin polymerization during airway smooth muscle contraction is unknown. Results: VASP activity requires phosphorylation at Ser157, recruitment to the membrane, and interaction with activated vinculin. Conclusion: VASP regulates actin polymerization and contraction in smooth muscle by a unique mechanism. Significance: The mechanism of VASP function is important for understanding actin dynamics in cells.

AB - Background: The function of vasodilator-stimulated phosphoprotein (VASP) in regulating actin polymerization during airway smooth muscle contraction is unknown. Results: VASP activity requires phosphorylation at Ser157, recruitment to the membrane, and interaction with activated vinculin. Conclusion: VASP regulates actin polymerization and contraction in smooth muscle by a unique mechanism. Significance: The mechanism of VASP function is important for understanding actin dynamics in cells.

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