ArticleG3 (Bethesda, Md.)2013
Fosmid-based structure-function analysis reveals functionally distinct domains in the cytoplasmic domain of Drosophila crumbs.
Article in G3 (Bethesda, Md.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Arc controls organ architecture through modulation of Crb and MyoII.The Journal of cell biology · 2025Article
- Pak1 and PP2A antagonize aPKC function to support cortical tension induced by the Crumbs-Yurt complex.eLife · 2021Article
- The cytoskeletal motor proteins Dynein and MyoV direct apical transport of Crumbs.Developmental biology · 2020Article
- The Crumbs3 Polarity Protein.Cold Spring Harbor perspectives in biology · 2018Review
- A dual role of the extracellular domain ofBiology open · 2018Article
- Distinct functions of Crumbs regulating slit diaphragms and endocytosis in Drosophila nephrocytes.Cellular and molecular life sciences : CMLS · 2017Article
- EPEC effector EspF promotes Crumbs3 endocytosis and disrupts epithelial cell polarity.Cellular microbiology · 2017Article
- Review
- The Crumbs_C isoform ofBiology open · 2017Article
- Article
- A Conserved Di-Basic Motif of Drosophila Crumbs Contributes to Efficient ER Export.Traffic (Copenhagen, Denmark) · 2015Article
- Localization and Function of Pals1-associated Tight Junction Protein in Drosophila Is Regulated by Two Distinct Apical Complexes.The Journal of biological chemistry · 2015Article
- The transmembrane protein Crumbs displays complex dynamics during follicular morphogenesis and is regulated competitively by Moesin and aPKC.Development (Cambridge, England) · 2015Article
- Structural basis for the phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein crumbs and the actin-binding protein moesin.The Journal of biological chemistry · 2015Article
- The C. elegans Crumbs family contains a CRB3 homolog and is not essential for viability.Biology open · 2015Article
- Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem reveals a highly specific assembly mechanism for the apical Crumbs complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Sticking together the Crumbs - an unexpected function for an old friend.Nature reviews. Molecular cell biology · 2013Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The evolutionarily conserved transmembrane protein Crumbs is required for epithelial polarity and morphogenesis in the embryo, control of tissue size in imaginal discs and morphogenesis of photoreceptor cells, and prevents light-dependent retinal degeneration. The small cytoplasmic domain contains two highly conserved regions, a FERM (i.e., protein 4.1/ezrin/radixin/moesin)-binding and a PDZ (i.e., postsynaptic density/discs large/ZO-1)-binding domain. Using a fosmid-based transgenomic approach, we analyzed the role of the two domains during invagination of the tracheae and the salivary glands in the Drosophila embryo. We provide data to show that the PDZ-binding domain is essential for the maintenance of cell polarity in both tissues. In contrast, in embryos expressing a Crumbs protein with an exchange of a conserved Tyrosine residue in the FERM-binding domain to an Alanine, both tissues are internalized, despite some initial defects in apical constriction, phospho-Moesin recruitment, and coordinated invagination movements. However, at later stages these embryos fail to undergo dorsal closure, germ band retraction, and head involution. In addition, frequent defects in tracheal fusion were observed. These results suggest stage and/or tissue specific binding partners. We discuss the power of this fosmid-based system for detailed structure-function analyses in comparison to the UAS/Gal4 system.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.