Assembly of Bazooka polarity landmarks through a multifaceted membrane-association mechanism.

Abstract:

:Epithelial cell polarity is essential for animal development. The scaffold protein Bazooka (Baz/PAR-3) forms apical polarity landmarks to organize epithelial cells. However, it is unclear how Baz is recruited to the plasma membrane and how this is coupled with downstream effects. Baz contains an oligomerization domain, three PDZ domains, and binding regions for the protein kinase aPKC and phosphoinositide lipids. With a structure-function approach, we dissected the roles of these domains in the localization and function of Baz in the Drosophila embryonic ectoderm. We found that a multifaceted membrane association mechanism localizes Baz to the apical circumference. Although none of the Baz protein domains are essential for cortical localization, we determined that each contributes to cortical anchorage in a specific manner. We propose that the redundancies involved might provide plasticity and robustness to Baz polarity landmarks. We also identified specific downstream effects, including the promotion of epithelial structure, a positive-feedback loop that recruits aPKC, PAR-6 and Crumbs, and a negative-feedback loop that regulates Baz.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

McKinley RF,Yu CG,Harris TJ

doi

10.1242/jcs.091884

subject

Has Abstract

pub_date

2012-03-01 00:00:00

pages

1177-90

issue

Pt 5

eissn

0021-9533

issn

1477-9137

pii

jcs.091884

journal_volume

125

pub_type

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