New insights into apical-basal polarization in epithelia

Riga, Amalia; Castiglioni, Victoria G; Boxem, Mike

doi:10.1016/j.ceb.2019.07.017

Cited by 54 publications

(42 citation statements)

References 78 publications

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“…Our work highlights previously unappreciated specificity in these activities, and begins to define the molecular functions of Scrib, Dlg, and Lgl. Our data focus on the Drosophila follicle epithelium, as well as in some cases Drosophila embryos, but it is important to note that tissue contexts can differ in polarity programs (18,56): For example, in the adult Drosophila midgut epithelium, where Scrib module proteins are dispensable for epithelial organization (29). We failed to detect phenotypic enhancement in double-mutant follicle cells, compared to single mutants, which together with the complete penetrance of single-mutant phenotypes suggest full codependence of function rather than functional overlap.…”

Section: Discussionmentioning

confidence: 99%

Distinct activities of Scrib module proteins organize epithelial polarity

Khoury

Bilder

2020

Proc. Natl. Acad. Sci. U.S.A.

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A polarized architecture is central to both epithelial structure and function. In many cells, polarity involves mutual antagonism between the Par complex and the Scribble (Scrib) module. While molecular mechanisms underlying Par-mediated apical determination are well-understood, how Scrib module proteins specify the basolateral domain remains unknown. Here, we demonstrate dependent and independent activities of Scrib, Discs-large (Dlg), and Lethal giant larvae (Lgl) using theDrosophilafollicle epithelium. Our data support a linear hierarchy for localization, but rule out previously proposed protein–protein interactions as essential for polarization. Cortical recruitment of Scrib does not require palmitoylation or polar phospholipid binding but instead an independent cortically stabilizing activity of Dlg. Scrib and Dlg do not directly antagonize atypical protein kinase C (aPKC), but may instead restrict aPKC localization by enabling the aPKC-inhibiting activity of Lgl. Importantly, while Scrib, Dlg, and Lgl are each required, all three together are not sufficient to antagonize the Par complex. Our data demonstrate previously unappreciated diversity of function within the Scrib module and begin to define the elusive molecular functions of Scrib and Dlg.

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Section: Discussionmentioning

confidence: 99%

Distinct activities of Scrib module proteins organize epithelial polarity

Khoury

Bilder

2020

Proc. Natl. Acad. Sci. U.S.A.

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“…TJs are composed of occludin, claudins, and JAMs (Junctional Adhesion Molecules) that are linked to the actin cytoskeleton through ZO (zonulae occludens) proteins [2]. Apical-basal polarity is controlled by: 1) the apical complex-the PAR proteins PAR3 and PAR6, aPKC, the CDC42 GTPase, the CRUMBS complex (CRUMBS, PALS1, PATJ, and LIN-7); 2) the basolateral complex (SCRIB, DLG, LGL); and 3) a cytoplasmic group of polarity proteins-PAR4/LKB1, PAR1/MARK, PAR5/14-3-3 [3]. Multi-level regulatory interactions between polarity proteins are essential for establishing and maintaining cell polarity.…”

Section: Epithelial Cellsmentioning

confidence: 99%

Phenotypic Plasticity of Cancer Cells Based on Remodeling of the Actin Cytoskeleton and Adhesive Structures

Rubtsova¹,

Zhitnyak²,

Gloushankova³

2021

IJMS

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There is ample evidence that, instead of a binary switch, epithelial-mesenchymal transition (EMT) in cancer results in a flexible array of phenotypes, each one uniquely suited to a stage in the invasion-metastasis cascade. The phenotypic plasticity of epithelium-derived cancer cells gives them an edge in surviving and thriving in alien environments. This review describes in detail the actin cytoskeleton and E-cadherin-based adherens junction rearrangements that cancer cells need to implement in order to achieve the advantageous epithelial/mesenchymal phenotype and plasticity of migratory phenotypes that can arise from partial EMT.

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“…Thus, it is logical to consider that the biogenesis of specific membrane polar cargoes destined to the fungal apical region might differ mechanistically with that of transporters, localized non-polarly all along the PM (Figure 1). The distinct localization of fungal membrane cargoes might present some analogies to distinct cargo localization in basolateral and apical membranes in metazoa [68,69]. In all cases, the simplest scenario is that cargoes themselves contain intrinsic information for distinct subcellular localization.…”

Section: Do Transporters Reach the Pm Via Conventional Golgi-dependenmentioning

confidence: 99%

Life and Death of Fungal Transporters under the Challenge of Polarity

Dimou

Diallinas

2020

IJMS

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Eukaryotic plasma membrane (PM) transporters face critical challenges that are not widely present in prokaryotes. The two most important issues are proper subcellular traffic and targeting to the PM, and regulated endocytosis in response to physiological, developmental, or stress signals. Sorting of transporters from their site of synthesis, the endoplasmic reticulum (ER), to the PM has been long thought, but not formally shown, to occur via the conventional Golgi-dependent vesicular secretory pathway. Endocytosis of specific eukaryotic transporters has been studied more systematically and shown to involve ubiquitination, internalization, and sorting to early endosomes, followed by turnover in the multivesicular bodies (MVB)/lysosomes/vacuole system. In specific cases, internalized transporters have been shown to recycle back to the PM. However, the mechanisms of transporter forward trafficking and turnover have been overturned recently through systematic work in the model fungus Aspergillus nidulans. In this review, we present evidence that shows that transporter traffic to the PM takes place through Golgi bypass and transporter endocytosis operates via a mechanism that is distinct from that of recycling membrane cargoes essential for fungal growth. We discuss these findings in relation to adaptation to challenges imposed by cell polarity in fungi as well as in other eukaryotes and provide a rationale of why transporters and possibly other housekeeping membrane proteins ‘avoid’ routes of polar trafficking.

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New insights into apical-basal polarization in epithelia

Cited by 54 publications

References 78 publications

Distinct activities of Scrib module proteins organize epithelial polarity

Distinct activities of Scrib module proteins organize epithelial polarity

Phenotypic Plasticity of Cancer Cells Based on Remodeling of the Actin Cytoskeleton and Adhesive Structures

Life and Death of Fungal Transporters under the Challenge of Polarity

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