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Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-Cadherin endocytosis

Background - Integral to the function and morphology of the epithelium is the lattice of cell-cell junctions known as adherens junctions (AJs). AJ stability and plasticity relies on E-Cadherin exocytosis and endocytosis. A mechanism regulating E-Cadherin (E-Cad) exocytosis to the AJs has implicated...

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Main Authors: Leibfried, Andrea (Author) , Fricke, Robert Patrick (Author) , Morgan, Matthew J. (Author) , Bogdan, Sven (Author) , Bellaïche, Yohanns (Author)
Format: Article (Journal)
Language:English
Published: November 2008
In: Current biology
Year: 2008, Volume: 18, Issue: 21, Pages: 1639-1648
ISSN:1879-0445
DOI:10.1016/j.cub.2008.09.063
Online Access:Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.cub.2008.09.063
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0960982208013419
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Author Notes:Andrea Leibfried, Robert Fricke, Matthew J. Morgan, Sven Bogdan, and Yohanns Bellaiche

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520 |a Background - Integral to the function and morphology of the epithelium is the lattice of cell-cell junctions known as adherens junctions (AJs). AJ stability and plasticity relies on E-Cadherin exocytosis and endocytosis. A mechanism regulating E-Cadherin (E-Cad) exocytosis to the AJs has implicated proteins of the exocyst complex, but mechanisms regulating E-Cad endocytosis from the AJs remain less well understood. - Results - Here we show that Cdc42, Par6, or aPKC loss of function is accompanied by the accumulation of apical E-Cad intracellular punctate structures and the disruption of AJs in Drosophila epithelial cells. These punctate structures derive from large and malformed endocytic vesicles that emanate from the AJs; a phenotype that is also observed upon blocking vesicle scission in dynamin mutant cells. We demonstrate that the Drosophila Cdc42-interacting protein 4 (Cip4) is a Cdc42 effector that interacts with Dynamin and the Arp2/3 activator WASp in Drosophila. Accordingly, Cip4, WASp, or Arp2/3 loss of function also results in defective E-Cadherin endocytosis. - Conclusion - Altogether our results show that Cdc42 functions with Par6 and aPKC to regulate E-Cad endocytosis and define Cip4 and WASp as regulators of the early E-Cad endocytic events in epithelial tissue. 
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