Faculty Opinions recommendation of Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.8224957.8645055 ◽

2011 ◽

Author(s):

Valeri Vasioukhin ◽

Smitha Sripathy

Keyword(s):

Junction Formation ◽

Epithelial Junctions

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Faculty Opinions recommendation of Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.8224957.9666057 ◽

2011 ◽

Author(s):

Alan Fanning ◽

Laurel Rodgers

Keyword(s):

Junction Formation ◽

Epithelial Junctions

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Paracingulin Regulates the Activity of Rac1 and RhoA GTPases by Recruiting Tiam1 and GEF-H1 to Epithelial Junctions

Molecular Biology of the Cell ◽

10.1091/mbc.e08-06-0558 ◽

2008 ◽

Vol 19 (10) ◽

pp. 4442-4453 ◽

Cited By ~ 58

Author(s):

Laurent Guillemot ◽

Serge Paschoud ◽

Lionel Jond ◽

Andrea Foglia ◽

Sandra Citi

Keyword(s):

Tight Junction ◽

Small Gtpases ◽

Cell Junctions ◽

Dependent Manner ◽

Junction Protein ◽

Junction Formation ◽

Epithelial Junctions ◽

Junctional Protein

Small GTPases control key cellular events, including formation of cell–cell junctions and gene expression, and are regulated by activating and inhibiting factors. Here, we characterize the junctional protein paracingulin as a novel regulator of the activity of two small GTPases, Rac1 and RhoA, through the functional interaction with their respective activators, Tiam1 and GEF-H1. In confluent epithelial monolayers, paracingulin depletion leads to increased RhoA activity and increased expression of mRNA for the tight junction protein claudin-2. During tight junction assembly by the calcium-switch, Rac1 shows two transient peaks of activity, at earlier (10–20 min) and later (3–8 h) time points. Paracingulin depletion reduces such peaks of Rac1 activation in a Tiam1-dependent manner, resulting in a delay in junction formation. Paracingulin physically interacts with GEF-H1 and Tiam1 in vivo and in vitro, and it is required for their efficient recruitment to junctions, based on immunofluorescence and biochemical experiments. Our results provide the first description of a junctional protein that interacts with GEFs for both Rac1 and RhoA, and identify a novel molecular mechanism whereby Rac1 is activated during junction formation.

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