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Abstract

Cell polarity is defined as asymmetry in cell shape, protein distributions and cell functions. It is characteristic of single-cell organisms, including yeast and bacteria, and cells in tissues of multi-cell organisms such as epithelia in worms, flies and mammals. This diversity raises several questions: do different cell types use different mechanisms to generate polarity, how is polarity signalled, how do cells react to that signal, and how is structural polarity translated into specialized functions? Analysis of evolutionarily diverse cell types reveals that cell-surface landmarks adapt core pathways for cytoskeleton assembly and protein transport to generate cell polarity.

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Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors.

D Bilder, M. Li, N Perrimon (2000)

Loss of cell polarity and tissue architecture are characteristics of malignant cancers derived from epithelial tissues. We provide evidence from Drosophila that a group of membrane-associated proteins act in concert to regulate both epithelial structure and cell proliferation. Scribble (Scrib) is a cell junction-localized protein required for polarization of embryonic and, as demonstrated here, imaginal disc and follicular epithelia. We show that the tumor suppressors lethal giant larvae (lgl) and discs-large (dlg) have identical effects on all three epithelia, and that scrib also acts as a tumor suppressor. Scrib and Dlg colocalize and overlap with Lgl in epithelia; activity of all three genes is required for cortical localization of Lgl and junctional localization of Scrib and Dlg. scrib, dlg, and lgl show strong genetic interactions. Our data indicate that the three tumor suppressors act together in a common pathway to regulate cell polarity and growth control.

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The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42.

G Joberty, C. Petersen, L Gao … (2000)

PAR (partitioning-defective) proteins, which were first identified in the nematode Caenorhabditis elegans, are essential for asymmetric cell division and polarized growth, whereas Cdc42 mediates establishment of cell polarity. Here we describe an unexpected link between these two systems. We have identified a family of mammalian Par6 proteins that are similar to the C. elegans PDZ-domain protein PAR-6. Par6 forms a complex with Cdc42-GTP, with a human homologue of the multi-PDZ protein PAR-3 and with the regulatory domains of atypical protein kinase C (PKC) proteins. This assembly is implicated in the formation of normal tight junctions at epithelial cell-cell contacts. Thus, Par6 is a key adaptor that links Cdc42 and atypical PKCs to Par3.

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Localization of apical epithelial determinants by the basolateral PDZ protein Scribble.

D Bilder, N Perrimon (2000)

The generation of membrane domains with distinct protein constituents is a hallmark of cell polarization. In epithelia, segregation of membrane proteins into apical and basolateral compartments is critical for cell morphology, tissue physiology and cell signalling. Drosophila proteins that confer apical membrane identity have been found, but the mechanisms that restrict these determinants to the apical cell surface are unknown. Here we show that a laterally localized protein is required for the apical confinement of polarity determinants. Mutations in Drosophila scribble (scrib), which encodes a multi-PDZ (PSD-95, Discs-large and ZO-1) and leucine-rich-repeat protein, cause aberrant cell shapes and loss of the monolayer organization of embryonic epithelia. Scrib is localized to the epithelial septate junction, the analogue of the vertebrate tight junction, at the boundary of the apical and basolateral cell surfaces. Loss of scrib function results in the misdistribution of apical proteins and adherens junctions to the basolateral cell surface, but basolateral protein localization remains intact. These phenotypes can be accounted for by mislocalization of the apical determinant Crumbs. Our results show that the lateral domain of epithelia, particularly the septate junction, functions in restricting apical membrane identity and correctly placing adherens junctions.

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PubMed ID:: 12700771

PMC ID:: 3373010

DOI:: 10.1038/nature01602

ScienceOpen disciplines: Chemistry

Keywords: Animals,Cell Polarity,Cell Size,Cytoskeleton,chemistry,metabolism,Epithelial Cells,cytology,Mitosis,Protein Transport,Signal Transduction

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ScienceOpen disciplines: Chemistry

Keywords: Animals, Cell Polarity, Cell Size, Cytoskeleton, chemistry, metabolism, Epithelial Cells, cytology, Mitosis, Protein Transport, Signal Transduction

Adaptation of core mechanisms to generate cell polarity.

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Abstract

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Photoluminescent Nanomaterials

Most cited references 88

Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors.

The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42.

Localization of apical epithelial determinants by the basolateral PDZ protein Scribble.

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