Su(dx) E3 ubiquitin ligase–dependent and –independent functions of Polychaetoid, the Drosophila ZO-1 homologue
Autor: | Hideyuki Shimizu, Alexandre Djiane, Martin D. Jennings, Sarah J. Bray, Marian B. Wilkin, Sabine Mazleyrat, Martin Baron, Johanna M. Avis |
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Jazyk: | angličtina |
Rok vydání: | 2011 |
Předmět: |
Proline
Ubiquitin-Protein Ligases Notch signaling pathway Plasma protein binding Biology Article Adherens junction WW domain 03 medical and health sciences Structure-Activity Relationship 0302 clinical medicine Animals Drosophila Proteins Wings Animal Research Articles Alleles 030304 developmental biology 0303 health sciences Tight Junction Proteins Receptors Notch Sequence Homology Amino Acid Stem Cells Ovary Membrane Proteins Sense Organs Cell Biology Adherens Junctions Phosphoproteins Molecular biology Cell biology Ubiquitin ligase Protein Structure Tertiary Drosophila melanogaster Membrane protein Mutation biology.protein Zonula Occludens-1 Protein Female Signal transduction 030217 neurology & neurosurgery Drosophila Protein Protein Binding Signal Transduction |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
Popis: | Polychaetoid coordinates receptor trafficking and signaling with adherens junction organization. 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. |
Databáze: | OpenAIRE |
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