Tropomyosin isoforms support actomyosin biogenesis to generate contractile tension at the epithelial zonula adherens

Caldwell, Benjamin J., Lucas, Christine, Kee, Anthony J., Gaus, Katharina, Gunning, Peter W., Hardeman, Edna C., Yap, Alpha S. and Gomez, Guillermo A. (2014) Tropomyosin isoforms support actomyosin biogenesis to generate contractile tension at the epithelial zonula adherens. Cytoskeleton, 71 12: 663-676. doi:10.1002/cm.21202


Author Caldwell, Benjamin J.
Lucas, Christine
Kee, Anthony J.
Gaus, Katharina
Gunning, Peter W.
Hardeman, Edna C.
Yap, Alpha S.
Gomez, Guillermo A.
Title Tropomyosin isoforms support actomyosin biogenesis to generate contractile tension at the epithelial zonula adherens
Journal name Cytoskeleton   Check publisher's open access policy
ISSN 1949-3592
1949-3584
Publication date 2014-12
Year available 2014
Sub-type Article (original research)
DOI 10.1002/cm.21202
Open Access Status
Volume 71
Issue 12
Start page 663
End page 676
Total pages 14
Place of publication Hoboken, NJ, United States
Publisher John Wiley and Sons
Collection year 2015
Language eng
Abstract Epithelial cells generate contractile forces at their cell–cell contacts. These are concentrated at the specialized apical junction of the zonula adherens (ZA), where a ring of stabilized E-cadherin lies adjacent to prominent actomyosin bundles. Coupling of adhesion and actomyosin contractility yields tension in the junction. The biogenesis of junctional contractility requires actin assembly at the ZA as well as the recruitment of nonmuscle myosin II, but the molecular regulators of these processes are not yet fully understood. We now report a role for tropomyosins 5NM1 (Tm5NM1) and 5NM2 (Tm5NM2) in their generation. Both these tropomyosin isoforms were found at the ZA and their depletion by RNAi or pharmacological inhibition reduced both F-actin and myosin II content at the junction. Photoactivation analysis revealed that the loss of F-actin was attributable to a decrease in filament stability. These changes were accompanied by a decrease in E-cadherin content at junctions. Ultimately, both long-term depletion of Tm5NM1/2 and acute inhibition with drugs caused junctional tension to be reduced. Thus these tropomyosin isoforms are novel contributors to junctional contractility and integrity.
Keyword Actomyosin
Contractility
E-cadherin
Tropomyosin
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Published online 31 January 2015

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Institute for Molecular Bioscience - Publications
 
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