Document Detail


Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-cadherin endocytosis.
MedLine Citation:
PMID:  18976911     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Andrea Leibfried; Robert Fricke; Matthew J Morgan; Sven Bogdan; Yohanns Bellaiche
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-10-30
Journal Detail:
Title:  Current biology : CB     Volume:  18     ISSN:  0960-9822     ISO Abbreviation:  Curr. Biol.     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-11-12     Completed Date:  2009-02-03     Revised Date:  2012-06-18    
Medline Journal Info:
Nlm Unique ID:  9107782     Medline TA:  Curr Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1639-48     Citation Subset:  IM    
Affiliation:
Institut CURIE, Centre National de la Recherche, UMR 144, Equipe Polarité Cellulaire chez la Drosophile, 26 rue d'Ulm, 75248 Paris cedex 05, France.
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MeSH Terms
Descriptor/Qualifier:
Actin-Related Protein 2-3 Complex / metabolism
Actins / metabolism
Adherens Junctions / metabolism*
Animals
Cadherins / metabolism*
Carrier Proteins / metabolism
Drosophila / metabolism
Drosophila Proteins / metabolism*
Dynamins / metabolism
Endocytosis*
Epithelial Cells / metabolism
Protein Kinase C / metabolism*
Wiskott-Aldrich Syndrome Protein / metabolism
cdc42 GTP-Binding Protein / metabolism*
Chemical
Reg. No./Substance:
0/Actin-Related Protein 2-3 Complex; 0/Actins; 0/Cadherins; 0/Carrier Proteins; 0/Cip4 protein, Drosophila; 0/Drosophila Proteins; 0/WASp protein, Drosophila; 0/Wiskott-Aldrich Syndrome Protein; EC 2.7.11.13/PKC-3 protein; EC 2.7.11.13/Par-6 protein, Drosophila; EC 2.7.11.13/Protein Kinase C; EC 3.6.5.2/cdc42 GTP-Binding Protein; EC 3.6.5.5/Dynamins
Comments/Corrections
Comment In:
Curr Biol. 2008 Nov 11;18(21):R1014-7   [PMID:  19000799 ]

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