ArticleDevelopment (Cambridge, England)2014
The F-box protein Slmb restricts the activity of aPKC to polarize epithelial cells.
Article in Development (Cambridge, England), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed.
- Gene model for the ortholog ofbioRxiv : the preprint server for biology · 2026Article
- De Novo Missense Variants in FBXW11 Cause Diverse Developmental Phenotypes Including Brain, Eye, and Digit Anomalies.American journal of human genetics · 2019Article
- PKCζ and JNK signaling regulate radiation-induced compensatory proliferation in parotid salivary glands.PloS one · 2019Article
- Levels of Par-1 kinase determine the localization of Bruchpilot at the Drosophila neuromuscular junction synapses.Scientific reports · 2018Article
- The PAR proteins: from molecular circuits to dynamic self-stabilizing cell polarity.Development (Cambridge, England) · 2017Review
- Mechanisms of polarity protein expression control.Current opinion in cell biology · 2016Review
- Establishing and maintaining cell polarity with mRNA localization in Drosophila.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016Review
- Clustering and negative feedback by endocytosis in planar cell polarity signaling is modulated by ubiquitinylation of prickle.PLoS genetics · 2015Article
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Authors and funding
5 authors.
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Abstract
The Par-3/Par-6/aPKC complex is the primary determinant of apical polarity in epithelia across animal species, but how the activity of this complex is restricted to allow polarization of the basolateral domain is less well understood. In Drosophila, several multiprotein modules antagonize the Par complex through a variety of means. Here we identify a new mechanism involving regulated protein degradation. Strong mutations in supernumerary limbs (slmb), which encodes the substrate adaptor of an SCF-class E3 ubiquitin ligase, cause dramatic loss of polarity in imaginal discs accompanied by tumorous proliferation defects. Slmb function is required to restrain apical aPKC activity in a manner that is independent of endolysosomal trafficking and parallel to the Scribble module of junctional scaffolding proteins. The involvement of the Slmb E3 ligase in epithelial polarity, specifically limiting Par complex activity to distinguish the basolateral domain, points to parallels with polarization of the C. elegans zygote.
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