Arp2/3 promotes junction formation and maintenance in the<i>Caenorhabditis elegans</i>intestine by regulating membrane association of apical proteins

Bernadskaya, Yelena; Patel, Falshruti B.; Hsu, Hsiao-Ting; Soto, Martha C.

doi:10.1091/mbc.e10-10-0862

Cited by 54 publications

(77 citation statements)

References 55 publications

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“…9I,IЈ; 55,957±731, n5; P<0.0001 versus 82,186±1785 in WT, n5). In accordance with previous results (Bernadskaya et al, 2011;, a significant reduction of intestinal actin was also detectable in erm-1(tm677) embryos ( Fig. 9H,HЈ; 47,499±572, n5; P<0.0001 versus WT).…”

Section: Ifo-1 Interacts Genetically With Erm-1 and Dlg-1supporting

confidence: 93%

“…Development 139 (10) staining, but do not generally interfere with the apical localization of IFB-2 (Bernadskaya et al, 2011;Göbel et al, 2004;Patel et al, 2008;) (this study). Although IFO-1 and ERM-1 affect actin organization and distribution of IFs differently, depletion of both proteins enhances reduction of AFs and IFB-2 in the intestine.…”

Section: Research Articlesupporting

confidence: 49%

“…Lockwood et al, 2008) and reduction of apical F-actin (Bernadskaya et al, 2011). In ifo-1(kc2);dlg-1(RNAi) embryos, junctional pattern disruption was detectable (Fig.…”

Section: Research Articlementioning

confidence: 90%

“…The SAX-7 cytoplasmic tail contains three distinct consensus-binding sites, RGQNYPVSQR, SFIGQY and STFV, for cytoskeletal adaptor proteins (FERM: protein 4.1, ezrin, radixin, moesin), for ankyrin and for PDZ proteins (PSD95, DlgA, ZO-1), respectively (Zhou et al, 2008). Although loss of SAX-7 seems not to interfere with the junctional localization of the DAC (Bernadskaya et al, 2011), depletion of the DAC disturbs junctional localization of phosphorylated SAX-7 at the CeAJ in the intestine (our unpublished results). Very recently it has been demonstrated that HMR-1/E-cadherin and SAX-7/L1CAM also function redundantly in blastomere compaction and non-muscle myosin accumulation during C. elegans gastrulation (Grana et al, 2010).…”

Section: Research Articlementioning

confidence: 99%

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The novel intestinal filament organizer IFO-1 contributes to epithelial integrity in concert with ERM-1 and DLG-1

et al. 2012

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SUMMARYThe nematode Caenorhabditis elegans is an excellent model system in which to study in vivo organization and function of the intermediate filament (IF) system for epithelial development and function. Using a transgenic ifb-2::cfp reporter strain, a mutagenesis screen was performed to identify mutants with aberrant expression patterns of the IF protein IFB-2, which is expressed in a dense network at the subapical endotube just below the microvillar brush border of intestinal cells. Two of the isolated alleles (kc2 and kc3) were mapped to the same gene, which we refer to as ifo-1 (intestinal filament organizer). The encoded polypeptide colocalizes with IF proteins and F-actin in the intestine. The apical localization of IFO-1 does not rely on IFB-2 but is dependent on LET-413, a basolateral protein involved in apical junction assembly and maintenance of cell polarity. In mutant worms, IFB-2 and IFC-2 are mislocalized in cytoplasmic granules and accumulate in large aggregates at the C. elegans apical junction (CeAJ) in a DLG-1-dependent fashion. Electron microscopy reveals loss of the prominent endotube and disordered but still intact microvilli. Semiquantitative fluorescence microscopy revealed a significant decrease of F-actin, suggesting a general role of IFO-1 in cytoskeletal organization. Furthermore, downregulation of the cytoskeletal organizer ERM-1 and the adherens junction component DLG-1, each of which leads to F-actin reduction on its own, induces a novel synthetic phenotype in ifo-1 mutants resulting in disruption of the lumen. We conclude that IFO-1 is a multipurpose linker between different cytoskeletal components of the C. elegans intestinal terminal web and contributes to proper epithelial tube formation.

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Section: Ifo-1 Interacts Genetically With Erm-1 and Dlg-1supporting

confidence: 93%

Section: Research Articlesupporting

confidence: 49%

“…Lockwood et al, 2008) and reduction of apical F-actin (Bernadskaya et al, 2011). In ifo-1(kc2);dlg-1(RNAi) embryos, junctional pattern disruption was detectable (Fig.…”

Section: Research Articlementioning

confidence: 90%

Section: Research Articlementioning

confidence: 99%

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The novel intestinal filament organizer IFO-1 contributes to epithelial integrity in concert with ERM-1 and DLG-1

et al. 2012

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“…Dlg1 localization at the basolateral side of the intestinal epithelium requires CASK, another MAGUK protein, however dlg1 mutations there cannot affect epithelial polarity (Lozovatsky et al 2009). Data from the C. elegans intestinal epithelium show that Arp2/3, which promotes nucleation of branched actin, junction initiation and maturation, affects the subcellular distribution of Dlg (Bernadskaya et al 2011). Dlg, Scrib and Lgl are also important in follicular epithelium morphogenesis and subsequent polarization of the Drosophila oocyte, albeit in a different way as in other epithelia.…”

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confidence: 99%

Refining the role of Lgl, Dlg and Scrib in Tumor Suppression and Beyond: Learning from the Old Time Classics

Papagiannouli¹,

Mechler²

2012

Tumor Suppressor Genes

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The minus‐end actin capping protein, UNC‐94/tropomodulin, regulates development of the Caenorhabditis elegans intestine

Cox-Paulson

Cannataro

Gallagher

et al. 2014

Developmental Dynamics

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Background Tropomodulins are actin capping proteins that regulate the stability of the slow growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94 has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results In the embryonic C. elegans intestine, UNC-94 localizes to the terminal web, an actin and intermediate filament rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the terminal web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the terminal web. The non-muscle myosin, NMY-1, also localizes to the terminal web; and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the terminal web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis.

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Arp2/3 promotes junction formation and maintenance in theCaenorhabditis elegansintestine by regulating membrane association of apical proteins

Abstract: Arp2/3 is shown to positively regulate adherens junction development and maintenance in the Caenorhabditis elegans intestine. Arp2/3 regulation of ERM-1, a molecule that connects F-actin to membranes, is required for this process.

Cited by 54 publications

References 55 publications

The novel intestinal filament organizer IFO-1 contributes to epithelial integrity in concert with ERM-1 and DLG-1

The novel intestinal filament organizer IFO-1 contributes to epithelial integrity in concert with ERM-1 and DLG-1

Refining the role of Lgl, Dlg and Scrib in Tumor Suppression and Beyond: Learning from the Old Time Classics

The minus‐end actin capping protein, UNC‐94/tropomodulin, regulates development of the Caenorhabditis elegans intestine

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