The Rap GTPase Activator Drosophila PDZ-GEF Regulates Cell Shape in Epithelial Migration and Morphogenesis

Boettner, B., Van Aelst, L. (November 2007) The Rap GTPase Activator Drosophila PDZ-GEF Regulates Cell Shape in Epithelial Migration and Morphogenesis. Mol Cell Biol, 27 (22). pp. 7966-7980. ISSN 0270-7306 (Print)

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URL: https://www.ncbi.nlm.nih.gov/pubmed/17846121
DOI: 10.1128/mcb.01275-07

Abstract

Epithelial morphogenesis is characterized by an exquisite control of cell shape and position. Progression through dorsal closure in Drosophila gastrulation depends on the ability of Rap1 GTPase to signal through the adherens junctional multidomain protein Canoe. Here, we provide genetic evidence that epithelial Rap activation and Canoe effector usage is conferred by the dPDZ-GEF exchange factor. We demonstrate that dPDZ-GEF/Rap/Canoe signaling modulates cell shape and apicolateral cell constriction in embryonic and wing disc epithelia. In dPDZ-GEF mutant embryos with strong dorsal closure defects, cells in the lateral ectoderm fail to properly elongate. Postembryonic dPDZ-GEF mutant cells generated in mosaic tissue display a striking extension of lateral cell perimeters in the proximity of junctional complexes, suggesting a loss of normal cell contractility. Furthermore, our data indicate that dPDZ-GEF signaling is linked to Myosin II function. Both dPDZ-GEF and cno show strong genetic interactions with the Myosin II encoding gene and Myosin II distribution is severely perturbed in epithelia of both mutants. These findings provide first insight into the molecular machinery targeted by Rap signaling to modulate epithelial plasticity. We propose that dPDZ-GEF-dependent signaling functions as a rheostat linking Rap activity to the regulation of cell shape in epithelial morphogenesis at different developmental stages.

Item Type: Paper
Subjects: organism description > animal > insect > Drosophila
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > GTPase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > myosin
CSHL Authors:
Communities: CSHL labs > Van Aelst lab
Depositing User: CSHL Librarian
Date: November 2007
Date Deposited: 30 Nov 2011 21:48
Last Modified: 22 Feb 2017 17:31
PMCID: PMC2169160
Related URLs:
URI: http://repository.cshl.edu/id/eprint/22973

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