A Conserved Oligomerization Domain in Drosophila Bazooka/PAR-3 Is Important for Apical Localization and Epithelial Polarity

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 [1]. In each context, the components of this complex display a mutually dependent asymmetric cortical localization....

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Bibliographic Details
Published in:Current biology 2003-08, Vol.13 (15), p.1330-1334
Main Authors: Benton, Richard, Johnston, Daniel St
Format: Article
Language:English
Subjects:
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
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Summary: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 [1]. 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 [2]. Mammalian PAR-3 (mPar3) can associate with transmembrane proteins and may link the complex to the membrane [3-5], 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 [6] 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.
ISSN:0960-9822
1879-0445
DOI:10.1016/S0960-9822(03)00508-6