A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Djiane, A., Shimizu, H., Wilkin, M., Mazleyrat, S., Jennings, M.D., Avis, J., Bray, S., Baron, M. (2011). Su(dx) E3 ubiquitin ligase-dependent and -independent functions of Polychaetoid, the Drosophila ZO-1 homologue.  J. Cell Biol. 192(1): 189--200. (Export to RIS)
FlyBase ID FBrf0212737
Publication Type Research paper
PubMed ID 21200027
PubMed Abstract Zona occludens (ZO) proteins are molecular scaffolds localized to cell junctions, which regulate epithelial integrity in mammals. Using newly generated null alleles, we demonstrate that polychaetoid (pyd), the unique Drosophila melanogaster ZO homologue, regulates accumulation of adherens junction-localized receptors, such as Notch, although it is dispensable for epithelial polarization. Pyd positively regulates Notch signaling during sensory organ development but acts negatively on Notch to restrict the ovary germline stem cell niche. In both contexts, we identify a core antagonistic interaction between Pyd and the WW domain E3 ubiquitin ligase Su(dx). Pyd binds Su(dx) directly, in part through a noncanonical WW-binding motif. Pyd also restricts epithelial wing cell numbers to control adult wing shape, a function associated with the FERM protein Expanded and independent of Su(dx). As both Su(dx) and Expanded regulate trafficking, we propose that a conserved role of ZO proteins is to coordinate receptor trafficking and signaling with junctional organization.
DOI 10.1083/jcb.201007023
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Language of Publication English
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Publication Type Journal
Abbreviation J. Cell Biol.
Title Journal of Cell Biology
Publication Year 1966-
ISBN/ISSN 0021-9525
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