scholarly journals Identification of a bipartite focal adhesion localization signal in RhoU/Wrch-1, a Rho family GTPase that regulates cell adhesion and migration

2007 ◽  
Vol 99 (12) ◽  
pp. 701-716 ◽  
Author(s):  
Stéphane Ory ◽  
Hélène Brazier ◽  
Anne Blangy
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion ◽  
Cell Adhesion And Migration ◽  
Localization Signal ◽  
Rho Family ◽  
And Migration

scholarly journals FRL, a Novel Formin-Related Protein, Binds to Rac and Regulates Cell Motility and Survival of Macrophages

2000 ◽  
Vol 20 (18) ◽  
pp. 6872-6881 ◽  
Author(s):  
Shinri Yayoshi-Yamamoto ◽  
Ichiro Taniuchi ◽  
Takeshi Watanabe
Keyword(s):  
Cell Death ◽  
Cell Adhesion ◽  
Bone Marrow Cells ◽  
Apoptotic Cell ◽  
Small Gtpases ◽  
Apoptotic Cell Death ◽  
Cell Adhesion And Migration ◽  
Rho Family ◽  
And Migration ◽  
Related Proteins

ABSTRACT We have isolated a cDNA, frl(formin-related gene in leukocytes), a novel mammalian member of the formin gene family. The frlcDNA encodes a 160-kDa protein, FRL, that possesses FH1, FH2, and FH3 domains that are well conserved among other Formin-related proteins. An FRL protein is mainly localized in the cytosol and is highly expressed in spleen, lymph node, and bone marrow cells. Formin-related genes and proteins have been reported to play crucial roles in morphogenesis, cell polarity, and cytokinesis through interaction with Rho family small GTPases. FRL binds to Rac at its N-terminal region including the FH3 domain and associates with profilin at the FH1 domain. In a macrophage cell line, P388D1, overexpression of a truncated form of FRL containing only the FH3 domain (FH3-FRL) strongly inhibited cell adhesion to fibronectin and migration upon stimulation with a chemokine. Moreover, expression of the truncated FH3-FRL protein resulted in apoptotic cell death of P388D1 cells, suggesting that the truncated FH3-FRL protein may interfere with signals of FRL. Overexpression in the P388D1 cells of full-length FRL or of the truncated protein containing the FH3 and FH1 domains, with simultaneous expression of the truncated FH3-FRL protein, blocked apoptotic cell death and inhibition of cell adhesion and migration. These results suggest that FRL may play a role in the control of reorganization of the actin cytoskeleton in association with Rac and also in the regulation of the signal for cell survival.

scholarly journals Guiding cell adhesion and motility by modulating cross-linking and topographic properties of microgel arrays

PLoS ONE ◽  
2021 ◽  
Vol 16 (9) ◽  
pp. e0257495
Author(s):  
Janine Riegert ◽  
Alexander Töpel ◽  
Jana Schieren ◽  
Renee Coryn ◽  
Stella Dibenedetto ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Cell Migration ◽  
Cell Adhesion ◽  
Focal Adhesion ◽  
Sertoli Cells ◽  
Cellular Systems ◽  
Cross Linking ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
The Impact

Biomaterial-driven modulation of cell adhesion and migration is a challenging aspect of tissue engineering. Here, we investigated the impact of surface-bound microgel arrays with variable geometry and adjustable cross-linking properties on cell adhesion and migration. We show that cell migration is inversely correlated with microgel array spacing, whereas directionality increases as array spacing increases. Focal adhesion dynamics is also modulated by microgel topography resulting in less dynamic focal adhesions on surface-bound microgels. Microgels also modulate the motility and adhesion of Sertoli cells used as a model for cell migration and adhesion. Both focal adhesion dynamics and speed are reduced on microgels. Interestingly, Gas2L1, a component of the cytoskeleton that mediates the interaction between microtubules and microfilaments, is dispensable for the regulation of cell adhesion and migration on microgels. Finally, increasing microgel cross-linking causes a clear reduction of focal adhesion turnover in Sertoli cells. These findings not only show that spacing and rigidity of surface-grafted microgels arrays can be effectively used to modulate cell adhesion and motility of diverse cellular systems, but they also form the basis for future developments in the fields of medicine and tissue engineering.

Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration

Oncogene ◽  
2017 ◽  
Vol 36 (47) ◽  
pp. 6509-6517 ◽  
Author(s):  
Y-R Chen ◽  
H-C Chou ◽  
C-H Yang ◽  
H-Y Chen ◽  
Y-W Liu ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Cell Adhesion And Migration ◽  
And Migration

scholarly journals GAR22β regulates cell migration, sperm motility, and axoneme structure

2016 ◽  
Vol 27 (2) ◽  
pp. 277-294 ◽  
Author(s):  
Ivonne Gamper ◽  
David Fleck ◽  
Meltem Barlin ◽  
Marc Spehr ◽  
Sara El Sayad ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Motility ◽  
Focal Adhesion ◽  
Wild Type ◽  
Cell Adhesion And Migration ◽  
Cytoskeleton Remodeling ◽  
Focal Adhesion Turnover ◽  
And Migration ◽  
Noncanonical Amino Acid ◽  
Dependent Processes

Spatiotemporal cytoskeleton remodeling is pivotal for cell adhesion and migration. Here we investigated the function of Gas2-related protein on chromosome 22 (GAR22β), a poorly characterized protein that interacts with actin and microtubules. Primary and immortalized GAR22β−/− Sertoli cells moved faster than wild-type cells. In addition, GAR22β−/− cells showed a more prominent focal adhesion turnover. GAR22β overexpression or its reexpression in GAR22β−/− cells reduced cell motility and focal adhesion turnover. GAR22β–actin interaction was stronger than GAR22β–microtubule interaction, resulting in GAR22β localization and dynamics that mirrored those of the actin cytoskeleton. Mechanistically, GAR22β interacted with the regulator of microtubule dynamics end-binding protein 1 (EB1) via a novel noncanonical amino acid sequence, and this GAR22β–EB1 interaction was required for the ability of GAR22β to modulate cell motility. We found that GAR22β is highly expressed in mouse testes, and its absence resulted in reduced spermatozoa generation, lower actin levels in testes, and impaired motility and ultrastructural disorganization of spermatozoa. Collectively our findings identify GAR22β as a novel regulator of cell adhesion and migration and provide a foundation for understanding the molecular basis of diverse cytoskeleton-dependent processes.

X-linked inhibitor of apoptosis protein controls α5-integrin-mediated cell adhesion and migration

2010 ◽  
Vol 299 (2) ◽  
pp. H300-H309 ◽  
Author(s):  
Jongmin Kim ◽  
Sunyoung Ahn ◽  
Young-Gyu Ko ◽  
Yong Chool Boo ◽  
Sung-Gil Chi ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Endothelial Cell ◽  
Focal Adhesion ◽  
Inhibitor Of Apoptosis ◽  
Erk Activation ◽  
Caveolin 1 ◽  
Endothelial Cell Survival ◽  
Apoptosis Protein ◽  
Cell Adhesion And Migration ◽  
And Migration

The association of integrins with caveolin-1 regulates cell adhesion. However, the vascular ramifications of this association remain to be clearly determined. We recently reported that the X chromosome-linked inhibitor of apoptosis protein (XIAP)-caveolin-1 interaction is critical to endothelial cell survival. Thus, we hypothesized that XIAP performs a crucial function in integrin/caveolin-1-mediated endothelial cell survival. In this study, we demonstrated that XIAP is recruited into the α5-integrin complex via caveolin-1 binding and mediates cell adhesion. We also determined that XIAP is critical to shear stress-stimulated ERK activation in an α5-integrin-dependent manner but is not important to VEGF-induced ERK activation. This differential activation of ERK is partly attributable to unique localizations of the receptors. Furthermore, we confirmed that XIAP is an essential molecule in the efficient recruitment of focal adhesion kinase (FAK) into the α5-integrin-associated complex. This α5-integrin-caveolin-1-XIAP-FAK multicomplex regulates endothelial cell migration via a mechanism that involves shear-dependent ERK activation. Together, our results indicate that XIAP stabilizes the α5-integrin-associated focal adhesion complex, thereby further regulating endothelial cell adhesion and migration. The findings of this study provide us with greater insight into the molecular mechanisms underlying the control of vascular function by integrins.

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