Imperial College London
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Dr Chris Tomlinson

Faculty of Medicine, Department of Surgery & Cancer

Honorary Research Fellow
 
 
 
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Contact

 

chris.tomlinson

 
 
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Location

 

Burlington DanesHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Braga:2016:10.1038/ncomms13542,
author = {Braga, VMM},
doi = {10.1038/ncomms13542},
journal = {Nature Communications},
pages = {1--17},
title = {Defining functional interactions during biogenesis of epithelial junctions},
url = {http://dx.doi.org/10.1038/ncomms13542},
volume = {7},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Braga,VMM
DO  - 10.1038/ncomms13542
EP  - 17
PY  - 2016///
SN  - 2041-1723
SP  - 1
TI  - Defining functional interactions during biogenesis of epithelial junctions
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/ncomms13542
UR  - http://www.nature.com/ncomms/index.html
UR  - http://hdl.handle.net/10044/1/41258
VL  - 7
ER  -
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