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      Rho1 regulates adherens junction remodeling by promoting recycling endosome formation through activation of myosin II

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          Abstract

          Rho1 influences adherens junction remodeling in live Drosophila pupal eye epithelia by regulating the formation of DE-cadherin–containing, Rab11-positive recycling endosomes. This effect of Rho1 is mediated through Rok, but not MLCK, stimulation of myosin II activity and is independent of Rho1’s effects on actin remodeling.

          Abstract

          Once adherens junctions (AJs) are formed between polarized epithelial cells they must be maintained because AJs are constantly remodeled in dynamic epithelia. AJ maintenance involves endocytosis and subsequent recycling of E-cadherin to a precise location along the basolateral membrane. In the Drosophila pupal eye epithelium, Rho1 GTPase regulates AJ remodeling through Drosophila E-cadherin (DE-cadherin) endocytosis by limiting Cdc42/Par6/aPKC complex activity. We demonstrate that Rho1 also influences AJ remodeling by regulating the formation of DE-cadherin–containing, Rab11-positive recycling endosomes in Drosophila postmitotic pupal eye epithelia. This effect of Rho1 is mediated through Rok-dependent, but not MLCK-dependent, stimulation of myosin II activity yet independent of its effects upon actin remodeling. Both Rho1 and pMLC localize on endosomal vesicles, suggesting that Rho1 might regulate the formation of recycling endosomes through localized myosin II activation. This work identifies spatially distinct functions for Rho1 in the regulation of DE-cadherin–containing vesicular trafficking during AJ remodeling in live epithelia.

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          BAR domains as sensors of membrane curvature: the amphiphysin BAR structure.

          Brian J. Peter, Helen M. Kent, Ian Mills … (2004)
          The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
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            Regulation of cadherin-mediated adhesion in morphogenesis.

            Barry Gumbiner (2005)
            Cadherin cell-adhesion proteins mediate many facets of tissue morphogenesis. The dynamic regulation of cadherins in response to various extracellular signals controls cell sorting, cell rearrangements and cell movements. Cadherins are regulated at the cell surface by an inside-out signalling mechanism that is analogous to the integrins in platelets and leukocytes. Signal-transduction pathways impinge on the catenins (cytoplasmic cadherin-associated proteins), which transduce changes across the membrane to alter the state of the cadherin adhesive bond.
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              Cadherins in development: cell adhesion, sorting, and tissue morphogenesis.

              Jennifer Halbleib, W Nelson (2006)
              Tissue morphogenesis during development is dependent on activities of the cadherin family of cell-cell adhesion proteins that includes classical cadherins, protocadherins, and atypical cadherins (Fat, Dachsous, and Flamingo). The extracellular domain of cadherins contains characteristic repeats that regulate homophilic and heterophilic interactions during adhesion and cell sorting. Although cadherins may have originated to facilitate mechanical cell-cell adhesion, they have evolved to function in many other aspects of morphogenesis. These additional roles rely on cadherin interactions with a wide range of binding partners that modify their expression and adhesion activity by local regulation of the actin cytoskeleton and diverse signaling pathways. Here we examine how different members of the cadherin family act in different developmental contexts, and discuss the mechanisms involved.
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                Author and article information

                Contributors
                Richard Fehon: Role: Monitoring Editor
                Journal
                Journal ID (nlm-ta): Mol Biol Cell
                Journal ID (iso-abbrev): Mol. Biol. Cell
                Journal ID (hwp): molbiolcell
                Journal ID (pmc): mbc
                Journal ID (publisher-id): Mol. Bio. Cell
                Title: Molecular Biology of the Cell
                Publisher: The American Society for Cell Biology
                ISSN (Print): 1059-1524
                ISSN (Electronic): 1939-4586
                Publication date (Print): 01 October 2014
                Volume: 25
                Issue: 19
                Pages: 2956-2969
                Affiliations
                [1] aICCE Institute, Washington University School of Medicine, St. Louis, MO 63110
                [2] bDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110
                [3] cDepartment of Developmental Biology, Washington University School of Medicine, St. Louis, MO 63110
                [4] dDepartment of Genetics, Washington University School of Medicine, St. Louis, MO 63110
                [5] eDepartment of Medicine, Washington University School of Medicine, St. Louis, MO 63110
                [6] fBRIGHT Institute, Washington University School of Medicine, St. Louis, MO 63110
                University of Chicago
                Author notes
                1Address correspondence to: Gregory D. Longmore ( glongmor@ 123456dom.wustl.edu ).
                Article
                Publisher ID: E14-04-0894
                DOI: 10.1091/mbc.E14-04-0894
                PMC ID: 4230585
                PubMed ID: 25079692
                SO-VID: 86fc75db-d180-4749-86a9-c98e881b56de
                Copyright © © 2014 Yashiro et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License ( http://creativecommons.org/licenses/by-nc-sa/3.0).
                License:

                “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.

                History
                Date received : 14 April 2014
                Date revision received : 14 July 2014
                Date accepted : 22 July 2014
                Categories
                Subject: Articles
                Subject: Cell Interactions

                ScienceOpen disciplines: Molecular biology
                Data availability:
                ScienceOpen disciplines: Molecular biology

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