scholarly journals Filopodia-based contact stimulation of cell migration drives tissue morphogenesis

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Maik C. Bischoff ◽  
Sebastian Lieb ◽  
Renate Renkawitz-Pohl ◽  
Sven Bogdan
Keyword(s):  
Adhesion Formation ◽  
Leading Edge ◽  
Free Edge ◽  
Dependent Manner ◽  
Cell Contacts ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Actin Cables ◽  
Cell Matrix Adhesion ◽  
Cell Cell

AbstractCells migrate collectively to form tissues and organs during morphogenesis. Contact inhibition of locomotion (CIL) drives collective migration by inhibiting lamellipodial protrusions at cell–cell contacts and promoting polarization at the leading edge. Here, we report a CIL-related collective cell behavior of myotubes that lack lamellipodial protrusions, but instead use filopodia to move as a cohesive cluster in a formin-dependent manner. We perform genetic, pharmacological and mechanical perturbation analyses to reveal the essential roles of Rac2, Cdc42 and Rho1 in myotube migration. These factors differentially control protrusion dynamics and cell–matrix adhesion formation. We also show that active Rho1 GTPase localizes at retracting free edge filopodia and that Rok-dependent actomyosin contractility does not mediate a contraction of protrusions at cell–cell contacts, but likely plays an important role in the constriction of supracellular actin cables. Based on these findings, we propose that contact-dependent asymmetry of cell–matrix adhesion drives directional movement, whereas contractile actin cables contribute to the integrity of the migrating cell cluster.

scholarly journals Filopodia-based contact stimulated collective migration drives tissue morphogenesis

2020 ◽  
Author(s):  
Maik C. Bischoff ◽  
Sebastian Lieb ◽  
Renate Renkawitz-Pohl ◽  
Sven Bogdan
Keyword(s):  
Adhesion Formation ◽  
Leading Edge ◽  
Dependent Manner ◽  
Collective Migration ◽  
Cell Contacts ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Actin Cables ◽  
Cell Matrix Adhesion ◽  
Cell Cell

AbstractCells migrate collectively to form tissues and organs during morphogenesis. Contact inhibition of locomotion (CIL) drives collective migration by inhibiting lamellipodial protrusions at cell-cell contacts and promoting polarization at the leading edge. Here, we report on a CIL-related collective cell behavior of myotubes that lack lamellipodial protrusions, but instead use filopodia to move as a cohesive cluster in a formin-dependent manner. Genetic, pharmacological and mechanical perturbation analyses reveal essential roles of Rac2, Cdc42 and Rho1 in myotube migration. They differentially control not only protrusion dynamics but also cell-matrix adhesion formation. Here, active Rho1 GTPase localizes at retracting free edge filopodia. Rok-dependent actomyosin contractility does not mediate a contraction of protrusions at cell-cell contacts but likely plays an important role in the constriction of supracellular actin cables.We propose that contact-dependent asymmetry of cell-matrix adhesion drives directional movement, whereas contractile actin cables contribute to the integrity of the migrating cell cluster.

scholarly journals Vascular Endothelial-Cadherin Regulates Cytoskeletal Tension, Cell Spreading, and Focal Adhesions by Stimulating RhoA

2004 ◽  
Vol 15 (6) ◽  
pp. 2943-2953 ◽  
Author(s):  
Celeste M. Nelson ◽  
Dana M. Pirone ◽  
John L. Tan ◽  
Christopher S. Chen
Keyword(s):  
Adhesion Formation ◽  
Focal Adhesions ◽  
Cell Spreading ◽  
Cell Contact ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Focal Adhesion Formation ◽  
Cytoskeletal Tension ◽  
Cell Matrix Adhesion ◽  
Cell Cell

Changes in vascular endothelial (VE)-cadherin–mediated cell-cell adhesion and integrin-mediated cell-matrix adhesion coordinate to affect the physical and mechanical rearrangements of the endothelium, although the mechanisms for such cross talk remain undefined. Herein, we describe the regulation of focal adhesion formation and cytoskeletal tension by intercellular VE-cadherin engagement, and the molecular mechanism by which this occurs. Increasing the density of endothelial cells to increase cell-cell contact decreased focal adhesions by decreasing cell spreading. This contact inhibition of cell spreading was blocked by disrupting VE-cadherin engagement with an adenovirus encoding dominant negative VE-cadherin. When changes in cell spreading were prevented by culturing cells on a micropatterned substrate, VE-cadherin–mediated cell-cell contact paradoxically increased focal adhesion formation. We show that VE-cadherin engagement mediates each of these effects by inducing both a transient and sustained activation of RhoA. Both the increase and decrease in cell-matrix adhesion were blocked by disrupting intracellular tension and signaling through the Rho-ROCK pathway. In all, these findings demonstrate that VE-cadherin signals through RhoA and the actin cytoskeleton to cross talk with cell-matrix adhesion and thereby define a novel pathway by which cell-cell contact alters the global mechanical and functional state of cells.

Ezrin regulates cell-cell and cell-matrix adhesion, a possible role with E-cadherin/beta-catenin

1999 ◽  
Vol 112 (18) ◽  
pp. 3081-3090 ◽  
Author(s):  
S. Hiscox ◽  
W.G. Jiang
Keyword(s):  
Cancer Cells ◽  
Focal Adhesions ◽  
Beta Catenin ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Ezrin Expression ◽  
Coated Surfaces ◽  
Cell Matrix Adhesion ◽  
E Cadherin ◽  
Cell Cell

Ezrin, radixin, moesin and merlin form a subfamily of conserved proteins in the band 4.1 superfamily. The function of these proteins is to link the plasma membrane to the actin cytoskeleton. Merlin is defective or absent in schwannomas and meningiomas and has been suggested to function as a tumour suppressor. In this study, we have examined the role of ezrin as a potential regulator of the adhesive and invasive behaviour of tumour cells. We have shown that following inhibition of ezrin expression in colo-rectal cancer cells using antisense oligonucleotides, these cells displayed a reduced cell-cell adhesiveness together with a gain in their motile and invasive behaviour. These cells also displayed increased spreading over matrix-coated surfaces. Immunofluorescence studies revealed that antisense-treated cells also displayed an increased staining of paxillin in areas representing focal adhesions. Furthermore, coprecipitation studies revealed an association of ezrin with E-cadherin and beta-catenin. Induction of the phosphorylation of ezrin by orthovanadate and hepatocyte growth factor/scatter factor resulted in changes similar to those seen with antisense treatment, together with a marked decrease in the association of ezrin with both beta-catenin and E-cadherin. It is concluded that ezrin regulates cell-cell and cell-matrix adhesion, by interacting with cell adhesion molecules E-cadherin and beta-catenin, and may thus play an important role in the control of adhesion and invasiveness of cancer cells.

scholarly journals Cell-matrix adhesion and cell-cell adhesion differentially control basal myosin oscillation and Drosophila egg chamber elongation

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Xiang Qin ◽  
Byung Ouk Park ◽  
Jiaying Liu ◽  
Bing Chen ◽  
Valerie Choesmel-Cadamuro ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Egg Chamber ◽  
Cell Matrix Adhesion ◽  
Cell Cell

XLMR protein related to neurite extension (Xpn/KIAA2022) regulates cell–cell and cell–matrix adhesion and migration

2013 ◽  
Vol 63 (6) ◽  
pp. 561-569 ◽  
Author(s):  
Takuya Magome ◽  
Tsuyoshi Hattori ◽  
Manabu Taniguchi ◽  
Toshiko Ishikawa ◽  
Shingo Miyata ◽  
...  
Keyword(s):  
Neurite Extension ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
And Migration ◽  
Cell Matrix Adhesion ◽  
Cell Cell

Regulation of cell???matrix adhesion and potentially also cell???cell adhesion by MIA

2006 ◽  
Vol 16 (Supplement 1) ◽  
pp. S18-S19
Author(s):  
A. Winklmeier ◽  
R. Bauer ◽  
S. Arndt ◽  
A. Bosserhoff
Keyword(s):  
Cell Adhesion ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion ◽  
Cell Cell

scholarly journals Alteration of Cell–Cell and Cell–Matrix Adhesion in Urothelial Cells: An Oncogenic Mechanism for Mutant FGFR3

2014 ◽  
Vol 13 (1) ◽  
pp. 138-148 ◽  
Author(s):  
Erica di Martino ◽  
Gavin Kelly ◽  
Jo-An Roulson ◽  
Margaret A. Knowles
Keyword(s):  
Urothelial Cells ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Cell Matrix Adhesion ◽  
Cell Cell

scholarly journals Preliminary evaluation of a Trypanosoma brucei FG-GAP repeat containing protein of mitochondrial localization

2019 ◽  
Vol 2 ◽  
pp. 165
Author(s):  
Monica Namyanja ◽  
Zhi-Shen Xu ◽  
Claire Mack Mugasa ◽  
Zhao-Rong Lun ◽  
Enock Matovu ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
Trypanosoma Brucei ◽  
Blood Brain Barrier ◽  
Brain Barrier ◽  
Preliminary Evaluation ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Blood Brain ◽  
Cell Matrix Adhesion ◽  
Cell Cell

Background: Trypanosoma brucei, a causative agent of African Trypanosomiasis, is known to cross the blood brain barrier during the second stage of the disease. It was previously suggested that this parasite crosses the blood brain barrier in a manner similar to that of lymphocytes. This would imply that trypanosomes possess integrins that are required to interact with adhesion molecules located on the blood brain barrier microvascular endothelial cells, as a first step in traversal. To date, no T. brucei integrin has been described. However, one T. brucei putative FG-GAP repeat containing protein (typical of integrins) encoded by the Tb927.11.720 gene, was predicted to be involved in cell-cell/cell-matrix adhesion. Therefore, this study sought to characterize a putative FG-GAP repeat containing protein (FG-GAP RCP) and to determine its cellular localization as a basis for further exploration of its potential role in cell-cell or cell-matrix adhesion. Methods: In this study, we successfully cloned, characterized, expressed and localized this protein using antibodies we produced against its VCBS domain in T. brucei. Results: Contrary to what we initially suspected, our data showed that this protein is localized to the mitochondria but not the plasma membrane. Our data showed that it contains putative calcium binding motifs within the FG-GAP repeats suggesting it could be involved in calcium signaling/binding in the mitochondrion of T. brucei. Conclusion: Based on its localization we conclude that this protein is unlikely to be a trypanosomal integrin and thus that it may not be involved in traversal of the blood brain barrier. However, it could be involved in calcium signaling in the mitochondrion.

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