The positioning and segregation of apical cues during epithelial polarity establishment in Drosophila
Open accessAbstract
Cell polarity is critical for epithelial structure and function. Adherens junctions (AJs) often direct this polarity, but we previously found that Bazooka (Baz) acts upstream of AJs as epithelial polarity is first established in Drosophila. This prompted us to ask how Baz is positioned and how downstream polarity is elaborated. Surprisingly, we found that Baz localizes to an apical domain below its typical binding partners atypical protein kinase C (aPKC) and partitioning defective (PAR)-6 as the Drosophila epithelium first forms. In fact, Baz positioning is independent of aPKC and PAR-6 relying instead on cytoskeletal cues, including an apical scaffold and dynein-mediated basal-to-apical transport. AJ assembly is closely coupled to Baz positioning, whereas aPKC and PAR-6 are positioned separately. This forms a stratified apical domain with Baz and AJs localizing basal to aPKC and PAR-6, and we identify specific mechanisms that keep these proteins apart. These results reveal key steps in the assembly of the apical domain in Drosophila.
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The dynein-dependent transport of the Drosophila Par3 homolog Bazooka is required for the segregation of apically localized proteins during the establishment of epithelial polarity.
“The dynein-dependent transport of the Drosophila Par3 homolog Bazooka is required for the segregation of apically localized proteins during the establishment of epithelial polarity (Harris and Peifer, 2005).”
From Rassf5 and Ndr kinases act in a novel pathway regulating neuronal polarity through Par3 phosphorylation (2014) · cites this paper as Harris and Peifer, 2005
The Results section ‘Baz positioning also requires dynein-mediated basal-to-apical transport’ supports dynein’s role in positioning Baz during cellularization. But ‘aPKC and PAR-6 positioning is dynein independent’ reports that apical and basal proteins still segregate in dynein mutants during gastrulation, contrary to the claim that dynein-dependent Baz transport is required for their segregation. (LLM, conf=0.87)
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- Authors
- Harris, T. J. C., & Peifer, M.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Peifer, Mark
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2005-08-29
- Volume
- 170
- Issue
- 5
- Pages
- 813-823
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2171335
- OpenAlex
- W2089839677
- Cited by
- 295
- References
- 44
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 5 · 2023: 5 · 2022: 13 · 2021: 12 · 2020: 13 · 2019: 16 · 2018: 12 · 2017: 20 · 2016: 13 · 2015: 16 · 2014: 10 · 2013: 13 · 2012: 24
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Institutes of Health
- Canadian Institutes of Health Research
- Natural Sciences and Engineering Research Council of Canada
- National Institute of General Medical Sciences (GM-47857, R01GM047857)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
- Keywords
- epithelial polarity, Bazooka, adherens junctions, apical domain, atypical protein kinase C, Par6, protein segregation
- MeSH terms
- Actins, Animals, Cytoskeleton, Drosophila melanogaster, Dyneins, Epithelial Cells, Membrane Proteins, Microtubules, Protein Kinase C, Proteins, Recombinant Fusion Proteins, Body Patterning, Protein Transport, Adherens Junctions, Drosophila Proteins, Intracellular Signaling Peptides and Proteins
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