Defining functional interactions during biogenesis of epithelial junctions

J. C. Erasmus, S. Bruche, L. Pizarro, N. Maimari, T. Poggioli, C. Tomlinson, J. Lees, I. Zalivina, A. Wheeler, A. Alberts, Angeloantonio Russo and V. M. M. Braga ()
Additional contact information
J. C. Erasmus: National Heart and Lung Institute, Faculty of Medicine, Imperial College London
S. Bruche: National Heart and Lung Institute, Faculty of Medicine, Imperial College London
L. Pizarro: National Heart and Lung Institute, Faculty of Medicine, Imperial College London
N. Maimari: National Heart and Lung Institute, Faculty of Medicine, Imperial College London
T. Poggioli: National Heart and Lung Institute, Faculty of Medicine, Imperial College London
C. Tomlinson: Faculty of Medicine, Imperial College London
J. Lees: University College London
I. Zalivina: National Heart and Lung Institute, Faculty of Medicine, Imperial College London
A. Wheeler: National Heart and Lung Institute, Faculty of Medicine, Imperial College London
A. Alberts: Van Andel Institute
V. M. M. Braga: National Heart and Lung Institute, Faculty of Medicine, Imperial College London

Nature Communications, 2016, vol. 7, issue 1, 1-17

Abstract: Abstract In spite of extensive recent progress, a comprehensive understanding of how actin cytoskeleton remodelling supports stable junctions remains to be established. Here we design a platform that integrates actin functions with optimized phenotypic clustering and identify new cytoskeletal proteins, their functional hierarchy and pathways that modulate E-cadherin adhesion. Depletion of EEF1A, an actin bundling protein, increases E-cadherin levels at junctions without a corresponding reinforcement of cell–cell contacts. This unexpected result reflects a more dynamic and mobile junctional actin in EEF1A-depleted cells. A partner for EEF1A in cadherin contact maintenance is the formin DIAPH2, which interacts with EEF1A. In contrast, depletion of either the endocytic regulator TRIP10 or the Rho GTPase activator VAV2 reduces E-cadherin levels at junctions. TRIP10 binds to and requires VAV2 function for its junctional localization. Overall, we present new conceptual insights on junction stabilization, which integrate known and novel pathways with impact for epithelial morphogenesis, homeostasis and diseases.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms13542 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13542

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms13542

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().