ArticleBioarchitecture2016
Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons.
Article in Bioarchitecture, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Lgl antagonizes Par complex membrane association to enable neural stem cell asymmetric division.Journal of cell science · 2026Article
- Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multisite polarity substrate Lgl.Nature structural & molecular biology · 2025Article
- Scribble, Lgl1, and myosin IIA interact with α-/β-catenin to maintain epithelial junction integrity.Cell adhesion & migration · 2023Article
- Endocytosis at the Crossroad of Polarity and Signaling Regulation: Learning fromInternational journal of molecular sciences · 2022Review
- Scribble, Lgl1, and myosin II form a complex in vivo to promote directed cell migration.Molecular biology of the cell · 2020Article
- Distinct activities of Scrib module proteins organize epithelial polarity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular asymmetries, often termed cell polarity, determine how cells organize and divide to ultimately control cell fate and shape animal tissues. The tumor suppressor Lethal giant larvae (Lgl) functions at the core of the evolutionarily conserved cell polarity machinery that controls apico-basal polarization. This function relies on its restricted basolateral localization via phosphorylation by aPKC. Here, we summarize the spatial and temporal control of Lgl during the cell cycle, highlighting two ideas that emerged from our recent findings: 1) Aurora A directly phosphorylates Lgl during symmetric division to couple reorganization of epithelial polarity with the cell cycle; 2) Phosphorylation of Lgl within three conserved serines controls its localization and function in a site-specific manner. Considering the importance of phosphorylation to regulate the concentration of Lgl at the plasma membrane, we will further discuss how it may work as an on-off switch for the interaction with cortical binding partners, with implications on epithelial polarization and spindle orientation.
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Registered trials
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.