A conserved oligomerization domain in drosophila Bazooka/PAR-3 is important for apical localization and epithelial polarity.

Détails

ID Serval
serval:BIB_DBBE3A288F9D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A conserved oligomerization domain in drosophila Bazooka/PAR-3 is important for apical localization and epithelial polarity.
Périodique
Current Biology
Auteur(s)
Benton R., St Johnston D.
ISSN
0960-9822[print], 0960-9822[linking]
Statut éditorial
Publié
Date de publication
2003
Volume
13
Numéro
15
Pages
1330-1334
Langue
anglais
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't Publication Status: ppublish
Résumé
The PAR-3/PAR-6/aPKC complex is required to establish polarity in many different cell types, including the C. elegans zygote and epithelial and neuronal cells in Drosophila and mammals. In each context, the components of this complex display a mutually dependent asymmetric cortical localization. PAR-6 is a direct effector of Rho family GTPases and binds to and regulates aPKC. Mammalian PAR-3 (mPar3) can associate with transmembrane proteins and may link the complex to the membrane, but this can account for only part of the requirement for this protein in the complex. Here we investigate the function of a novel conserved domain, CR1, of PAR-3 using computational, biochemical, and genetic approaches. Sequence-structure comparison by FUGUE predicts that CR1 has the same structural fold as a bacterial oligomerization domain. We show that CR1 of the Drosophila homolog, Bazooka (BAZ), mediates oligomerization in vitro and in vivo. Furthermore, deletion of CR1 disrupts BAZ localization in both epithelial cells and the germline and strongly impairs BAZ function in epithelial polarity. These results indicate that this domain is important for the localization and activity of the PAR-3/PAR6/aPKC complex and define a new role for PAR-3 in assembling higher order protein complexes.
Mots-clé
Amino Acid Sequence, Animals, Blotting, Western, Carrier Proteins/genetics, Carrier Proteins/metabolism, Cell Polarity/genetics, Chromosome Mapping, Conserved Sequence/genetics, Drosophila/embryology, Drosophila/genetics, Drosophila Proteins, Epithelial Cells, Gene Expression Profiling, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Precipitin Tests, Protein Binding, Two-Hybrid System Techniques
Pubmed
Web of science
Open Access
Oui
Création de la notice
18/03/2008 10:36
Dernière modification de la notice
20/08/2019 16:00
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