The Drosophila AIP orthologue is essential for actin cytoskeleton stabilisation and cell adhesion

2016 ◽  
Author(s):  
Elena Daniela Aflorei ◽  
Benjamin Klapholz ◽  
Nina Moderau ◽  
Paulo Baptista-Ribeiro ◽  
Nic Tapon ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton

Dynamic control of cell-cell adhesion and membrane-associated actin during food-induced mouth opening in Beroe

1993 ◽  
Vol 106 (1) ◽  
pp. 355-364
Author(s):  
S.L. Tamm ◽  
S. Tamm
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Actin Filaments ◽  
Dynamic Control ◽  
Mouth Opening ◽  
Cell Junctions ◽  
Dynamic Changes ◽  
Rhodamine Phalloidin ◽  
Rapid Changes ◽  
Muscular Action

We used rhodamine-phalloidin and ultrastructural methods to follow dynamic changes in adhesive cell junctions and associated actin filaments during reversible epithelial adhesion in the mouth of the ctenophore Beroe. A cruising Beroe keeps its mouth closed by interdigitated actin-coated appositions between paired strips of cells lining the lips. The mouth opens rapidly (in 0.2-0.3 s) by muscular action to engulf prey (other ctenophores), then re-seals after ingestion. We found that the interlocking surface architecture of the adhesive cells, including the actin-coated junctions, rapidly disappears after food-induced opening of the mouth. In contrast, forcible separation of the lips in the absence of food rips the junctions, still intact, from the surfaces of the cells. The prey-stimulated loss of adhesive cell junctions and associated actin cytoskeleton is one of the most rapid changes in actin-based junctions yet observed. This system provides unique experimental advantages for investigating the dynamic control of reversible cell adhesions and membrane-associated actin filaments.

Vascular-endothelial-cadherin modulates endothelial monolayer permeability

1999 ◽  
Vol 112 (12) ◽  
pp. 1915-1923 ◽  
Author(s):  
P.L. Hordijk ◽  
E. Anthony ◽  
F.P. Mul ◽  
R. Rientsma ◽  
L.C. Oomen ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Transendothelial Migration ◽  
Stress Fibers ◽  
Vascular Endothelial ◽  
Monolayer Permeability ◽  
Actin Stress Fibers ◽  
Cell Cell

Vascular endothelial (VE)-cadherin is the endothelium-specific member of the cadherin family of homotypic cell adhesion molecules. VE-cadherin, but not the cell adhesion molecule platelet/endothelial cell adhesion molecule (PECAM-1), markedly colocalizes with actin stress fibers at cell-cell junctions between human umbilical vein endothelial cells. Inhibition of VE-cadherin-mediated, but not PECAM-1-mediated, adhesion induced reorganization of the actin cytoskeleton, loss of junctional VE-cadherin staining and loss of cell-cell adhesion. In functional assays, inhibition of VE-cadherin caused increased monolayer permeability and enhanced neutrophil transendothelial migration. In a complementary set of experiments, modulation of the actin cytoskeleton was found to strongly affect VE-cadherin distribution. Brief stimulation of the beta2-adrenergic receptor with isoproterenol induced a loss of actin stress fibers resulting in a linear, rather than ‘jagged’, VE-cadherin distribution. The concomitant, isoproterenol-induced, reduction in monolayer permeability was alleviated by a VE-cadherin-blocking antibody. Finally, cytoskeletal reorganization resulting from the inactivation of p21Rho caused a diffuse localization of VE-cadherin, which was accompanied by reduced cell-cell adhesion. Together, these data show that monolayer permeability and neutrophil transendothelial migration are modulated by VE-cadherin-mediated cell-cell adhesion, which is in turn controlled by the dynamics of the actin cytoskeleton.

Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation

2002 ◽  
Vol 115 (12) ◽  
pp. 2581-2590 ◽  
Author(s):  
Françoise Coussen ◽  
Daniel Choquet ◽  
Michael P. Sheetz ◽  
Harold P. Erickson
Keyword(s):  
Cell Adhesion ◽  
Fluorescence Microscopy ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Fiber Bundles ◽  
Cell Surfaces ◽  
Actin Fiber ◽  
Filament Bundles ◽  
Necessary And Sufficient ◽  
Small Clusters

Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might be sufficient for activity. We have produced a monomer, three forms of dimers, a trimer and a pentamer of FN7-10,on the end of spacer arms. These oligomers could bind small clusters of up to five integrins. Fluorescence microscopy showed that the trimer and pentamer bound strongly to the cell surface, and within 5 minutes were prominently localized to actin fiber bundles. Monomers and dimers showed only diffuse localization. Beads coated with a low concentration (probably one complex per bead) of trimer or pentamer showed prolonged binding and rearward translocation, presumably with the translocating actin cytskeleton. Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton.

scholarly journals CD44 and β3 Integrin Organize Two Functionally Distinct Actin-based Domains in Osteoclasts

2007 ◽  
Vol 18 (12) ◽  
pp. 4899-4910 ◽  
Author(s):  
Anne Chabadel ◽  
Inmaculada Bañon-Rodríguez ◽  
David Cluet ◽  
Brian B. Rudkin ◽  
Bernhard Wehrle-Haller ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Interacting Protein ◽  
Wiskott Aldrich Syndrome ◽  
Diffuse Cloud ◽  
Sealing Zone ◽  
Β3 Integrin ◽  
Syndrome Protein

The actin cytoskeleton of mature osteoclasts (OCs) adhering to nonmineralized substrates is organized in a belt of podosomes reminiscent of the sealing zone (SZ) found in bone resorbing OCs. In this study, we demonstrate that the belt is composed of two functionally different actin-based domains: podosome cores linked with CD44, which are involved in cell adhesion, and a diffuse cloud associated with β3 integrin, which is involved in cell adhesion and contraction. Wiskott Aldrich Syndrome Protein (WASp) Interacting Protein (WIP)−/− OCs were devoid of podosomes, but they still exhibited actin clouds. Indeed, WIP−/− OCs show diminished expression of WASp, which is required for podosome formation. CD44 is a novel marker of OC podosome cores and the first nonintegrin receptor detected in these structures. The importance of CD44 is revealed by showing that its clustering restores podosome cores and WASp expression in WIP−/− OCs. However, although CD44 signals are sufficient to form a SZ, the presence of WIP is indispensable for the formation of a fully functional SZ.

scholarly journals The actin cytoskeleton and integrin expression in the recovery of cell adhesion after oxidant stress to a proximal tubule cell line (JTC-12).

1998 ◽  
Vol 9 (10) ◽  
pp. 1787-1797
Author(s):  
S Nigam ◽  
C E Weston ◽  
C H Liu ◽  
E E Simon
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Proximal Tubule ◽  
Cell Line ◽  
Oxidant Stress ◽  
Proximal Tubule Cell ◽  
Integrin Expression ◽  
Tubule Cell ◽  
Essentially Normal ◽  
Atp Levels

This study examines the role of the actin cytoskeleton and integrin expression in the recovery of cell adhesion in the proximal tubule cell line JTC-12 after peroxide injury. The cells were exposed to 10, 20, or 50 mM hydrogen peroxide for 10 min and then allowed to recover. Viability measurements by trypan blue exclusion confirmed that the injury was largely nonlethal with 85% viability at 1 h even at 50 mM peroxide. ATP levels fell immediately after the peroxide incubation in all groups to approximately 10% of normal, but already showed some recovery by 1 h and full recovery in the 10 and 20 mM groups by 24 h. Cell adhesion to extracellular matrix immediately after injury was depressed at 20 and 50 mM peroxide, but by 12 h was abnormal only at 50 mM peroxide and at 24 h was essentially normal at all peroxide concentrations. Immediately after exposure to 10 mM peroxide, there were subtle abnormalities in the actin cytoskeleton (thickening of fibrils) as assessed by phalloidin staining, with more pronounced effects at 20 and 50 mM. At 1 h, many cells showed collapse of the actin cytoskeleton to the periphery. There was some recovery at 4 h; by 12 h, the actin cytoskeleton showed further recovery, although was still abnormal (coarsened microfilaments), especially at 20 and 50 mM peroxide. By 24 h, the actin cytoskeleton showed only subtle coarsening. Integrin surface expression was assessed by flow cytometry. The alpha6 subunit on cells exposed to 20 mM peroxide was unchanged at 1 h and 4 h, but by 12 h had increased to 118.5+/-4.5% and by 24 h to 146+/-13.4% of control levels. The expression of the beta1 and alphaVbeta3 integrins remained unchanged. Thus, despite coarsening of the actin cytoskeleton and depressed ATP levels, cell adhesion recovered from oxidant stress. Abnormal cell adhesion after injury was not a consequence of a decrease in integrin expression, and recovery of cell adhesion was not a consequence of the modest and selective increase in integrin expression.

Samarium doped glass-reinforced hydroxyapatite with enhanced osteoblastic performance and antibacterial properties for bone tissue regeneration

2014 ◽  
Vol 2 (35) ◽  
pp. 5872-5881 ◽  
Author(s):  
Diana Santos Morais ◽  
João Coelho ◽  
Maria Pia Ferraz ◽  
Pedro Sousa Gomes ◽  
Maria Helena Fernandes ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Bone Tissue ◽  
Tissue Regeneration ◽  
Antibacterial Properties ◽  
Bone Tissue Regeneration ◽  
Osteoblastic Cells ◽  
Sem Images ◽  
Doped Glass

Cell adhesion of MG63 osteoblastic cells seeded over GR-HA_control and Sm doped composites, at day 1 of culture. Low (A) and high (B) CLSM images of cells stained for F-actin cytoskeleton (green) and nuclei (red); (C) SEM images.

scholarly journals α-Catenin-independent Recruitment of ZO-1 to Nectin-based Cell-Cell Adhesion Sites through Afadin

2001 ◽  
Vol 12 (6) ◽  
pp. 1595-1609 ◽  
Author(s):  
Shigekazu Yokoyama ◽  
Kouichi Tachibana ◽  
Hiroyuki Nakanishi ◽  
Yasunori Yamamoto ◽  
Kenji Irie ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Tight Junctions ◽  
Cell Lines ◽  
Adhesion Molecule ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Adhesion Sites ◽  
Cell Cell

ZO-1 is an actin filament (F-actin)–binding protein that localizes to tight junctions and connects claudin to the actin cytoskeleton in epithelial cells. In nonepithelial cells that have no tight junctions, ZO-1 localizes to adherens junctions (AJs) and may connect cadherin to the actin cytoskeleton indirectly through β- and α-catenins as one of many F-actin–binding proteins. Nectin is an immunoglobulin-like adhesion molecule that localizes to AJs and is associated with the actin cytoskeleton through afadin, an F-actin–binding protein. Ponsin is an afadin- and vinculin-binding protein that also localizes to AJs. The nectin-afadin complex has a potency to recruit the E-cadherin–β-catenin complex through α-catenin in a manner independent of ponsin. By the use of cadherin-deficient L cell lines stably expressing various components of the cadherin-catenin and nectin-afadin systems, and α-catenin–deficient F9 cell lines, we examined here whether nectin recruits ZO-1 to nectin-based cell-cell adhesion sites. Nectin showed a potency to recruit not only α-catenin but also ZO-1 to nectin-based cell-cell adhesion sites. This recruitment of ZO-1 was dependent on afadin but independent of α-catenin and ponsin. These results indicate that ZO-1 localizes to cadherin-based AJs through interactions not only with α-catenin but also with the nectin-afadin system.

scholarly journals Arginine deprivation affects glioblastoma cell adhesion, invasiveness and actin cytoskeleton organization by impairment of β-actin arginylation

Amino Acids ◽  
2014 ◽  
Vol 47 (1) ◽  
pp. 199-212 ◽  
Author(s):  
Iuliia Pavlyk ◽  
Yuriy Rzhepetskyy ◽  
Adam K. Jagielski ◽  
Jakub Drozak ◽  
Anna Wasik ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Glioblastoma Cell ◽  
Cytoskeleton Organization ◽  
Arginine Deprivation ◽  
Actin Cytoskeleton Organization

scholarly journals The type III TGFβ receptor regulates filopodia formation via a Cdc42-mediated IRSp53–N-WASP interaction in epithelial cells

2013 ◽  
Vol 454 (1) ◽  
pp. 79-89 ◽  
Author(s):  
Sun Young Oh ◽  
Erik H. Knelson ◽  
Gerard C. Blobe ◽  
Karthikeyan Mythreye
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Actin Cytoskeleton ◽  
Transforming Growth Factor ◽  
Small Gtpase ◽  
Mammary Epithelial ◽  
Migration And Invasion ◽  
Type Iii ◽  
Tgfβ Receptor

Cell adhesion and migration are tightly controlled by regulated changes in the actin cytoskeleton. Previously we reported that the TGFβ (transforming growth factor β) superfamily co-receptor, TβRIII (type III TGFβ receptor; also known as betaglycan), regulates cell adhesion, migration and invasion, and suppresses cancer progression, in part, through activation of the small GTPase Cdc42 (cell division cycle 42), and Cdc42-dependent alterations to the actin cytoskeleton. In the present study we demonstrate that TβRIII specifically promotes filopodial formation and extension in MCF10A and HMEC (human mammary epithelial cell) mammary epithelial cells. Mechanistically, cell-surface TβRIII and Cdc42 co-localize to filopodial structures and co-complex in a β-arrestin2-dependent, and a TβRI/TβRII-independent manner. The β-arrestin2-mediated interaction between TβRIII and Cdc42 increases complex formation between the Cdc42 effectors IRSp53 with N-WASP (neuronal Wiskott–Aldrich syndrome protein) to increase filopodial formation. We demonstrate a function link between filopodial structures and epithelial cell adhesion as regulated by the TβRIII–Cdc42 interaction. The present studies identify TβRIII as a novel regulator of IRSp53/N-WASP via Cdc42 to regulate filopodial formation and cell adhesion.

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