Literature DB >> 24067914

Evolution and cell physiology. 3. Using Dictyostelium discoideum to investigate mechanisms of epithelial polarity.

William I Weis1, W James Nelson, Daniel J Dickinson.   

Abstract

In Metazoa, a polarized epithelium forms a single-cell-layered barrier that separates the outside from the inside of the organism. In tubular epithelia, the apical side of the cell is constricted relative to the basal side, forming a wedge-shaped cell that can pack into a tube. Apical constriction is mediated by actomyosin activity. In higher animals, apical actomyosin is connected between cells by specialized cell-cell junctions that contain a classical cadherin, the Wnt signaling protein β-catenin, and the actin-binding protein α-catenin. The molecular mechanisms that lead to selective accumulation of myosin at the apical surface of cells are poorly understood. We found that the nonmetazoan Dictyostelium discoideum forms a polarized epithelium that surrounds the stalk tube at the tip of the multicellular fruiting body. Although D. discoideum lacks a cadherin homolog, it expresses homologs of β- and α-catenin. Both catenins are essential for formation of the tip epithelium, polarized protein secretion, and proper multicellular morphogenesis. Myosin localizes apically in tip epithelial cells, and it appears that constriction of this epithelial tube is required for proper morphogenesis. Localization of myosin II is controlled by the protein IQGAP1 and its binding partners cortexillins I and II, which function downstream of α- and β-catenin to exclude myosin from the basolateral cortex and promote apical accumulation of myosin. These studies show that the function of catenins in cell polarity predates the evolution of Wnt signaling and classical cadherins, and that apical localization of myosin is a morphogenetic mechanism conserved from nonmetazoans to vertebrates.

Entities:  

Keywords:  apical constriction; catenins; cell polarity; epithelium; evolution

Mesh:

Year:  2013        PMID: 24067914      PMCID: PMC3882382          DOI: 10.1152/ajpcell.00233.2013

Source DB:  PubMed          Journal:  Am J Physiol Cell Physiol        ISSN: 0363-6143            Impact factor:   4.249


  41 in total

1.  Recruitment of cortexillin into the cleavage furrow is controlled by Rac1 and IQGAP-related proteins.

Authors:  J Faix; I Weber; U Mintert; J Köhler; F Lottspeich; G Marriott
Journal:  EMBO J       Date:  2001-07-16       Impact factor: 11.598

Review 2.  Adaptation of core mechanisms to generate cell polarity.

Authors:  W James Nelson
Journal:  Nature       Date:  2003-04-17       Impact factor: 49.962

Review 3.  Sticky business: orchestrating cellular signals at adherens junctions.

Authors:  Mirna Perez-Moreno; Colin Jamora; Elaine Fuchs
Journal:  Cell       Date:  2003-02-21       Impact factor: 41.582

4.  Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1.

Authors:  S Kuroda; M Fukata; K Kobayashi; M Nakafuku; N Nomura; A Iwamatsu; K Kaibuchi
Journal:  J Biol Chem       Date:  1996-09-20       Impact factor: 5.157

5.  Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail.

Authors:  J Faix; M Steinmetz; H Boves; R A Kammerer; F Lottspeich; U Mintert; J Murphy; A Stock; U Aebi; G Gerisch
Journal:  Cell       Date:  1996-08-23       Impact factor: 41.582

Review 6.  Mechanosensitive systems at the cadherin-F-actin interface.

Authors:  Stephan Huveneers; Johan de Rooij
Journal:  J Cell Sci       Date:  2013-03-22       Impact factor: 5.285

7.  Adherens junctions and beta-catenin-mediated cell signalling in a non-metazoan organism.

Authors:  M J Grimson; J C Coates; J P Reynolds; M Shipman; R L Blanton; A J Harwood
Journal:  Nature       Date:  2000-12-07       Impact factor: 49.962

8.  Directed actin polymerization is the driving force for epithelial cell-cell adhesion.

Authors:  V Vasioukhin; C Bauer; M Yin; E Fuchs
Journal:  Cell       Date:  2000-01-21       Impact factor: 41.582

9.  The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin.

Authors:  A H Huber; W I Weis
Journal:  Cell       Date:  2001-05-04       Impact factor: 41.582

10.  Single amino acid substitutions in proteins of the armadillo gene family abolish their binding to alpha-catenin.

Authors:  H Aberle; H Schwartz; H Hoschuetzky; R Kemler
Journal:  J Biol Chem       Date:  1996-01-19       Impact factor: 5.157

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