scholarly journals The Cell Surface Hyaluronidase TMEM2 Regulates Cell Adhesion and Migration via Degradation of Hyaluronan at Focal Adhesion Sites

2021 ◽  
pp. 100481
Author(s):  
Fumitoshi Irie ◽  
Yuki Tobisawa ◽  
Ayako Murao ◽  
Hayato Yamamoto ◽  
Chikara Ohyama ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Focal Adhesion ◽  
Adhesion Sites ◽  
Cell Adhesion And Migration ◽  
And Migration

scholarly journals Ankyrin binding mediates L1CAM interactions with static components of the cytoskeleton and inhibits retrograde movement of L1CAM on the cell surface

2003 ◽  
Vol 162 (4) ◽  
pp. 719-730 ◽  
Author(s):  
Orlando D. Gil ◽  
Takeshi Sakurai ◽  
Ann E. Bradley ◽  
Marc Y. Fink ◽  
Melanie R. Cassella ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Crucial Role ◽  
Adaptor Protein ◽  
Axon Growth ◽  
Cell Adhesion And Migration ◽  
Dynamic Components ◽  
And Migration ◽  
Adhesive Contacts ◽  
Stationary Behavior

The function of adhesion receptors in both cell adhesion and migration depends critically on interactions with the cytoskeleton. During cell adhesion, cytoskeletal interactions stabilize receptors to strengthen adhesive contacts. In contrast, during cell migration, adhesion proteins are believed to interact with dynamic components of the cytoskeleton, permitting the transmission of traction forces through the receptor to the extracellular environment. The L1 cell adhesion molecule (L1CAM), a member of the Ig superfamily, plays a crucial role in both the migration of neuronal growth cones and the static adhesion between neighboring axons. To understand the basis of L1CAM function in adhesion and migration, we quantified directly the diffusion characteristics of L1CAM on the upper surface of ND-7 neuroblastoma hybrid cells as an indication of receptor–cytoskeleton interactions. We find that cell surface L1CAM engages in diffusion, retrograde movement, and stationary behavior, consistent with interactions between L1CAM and two populations of cytoskeleton proteins. We provide evidence that the cytoskeletal adaptor protein ankyrin mediates stationary behavior while inhibiting the actin-dependent retrograde movement of L1CAM. Moreover, inhibitors of L1CAM–ankyrin interactions promote L1CAM-mediated axon growth. Together, these results suggest that ankyrin binding plays a crucial role in the anti-coordinate regulation of L1CAM-mediated adhesion and migration.

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 CKAP4 Regulates Cell Migration via the Interaction with and Recycling of Integrin

2019 ◽  
Vol 39 (16) ◽  
Author(s):  
Yoshihito Osugi ◽  
Katsumi Fumoto ◽  
Akira Kikuchi
Keyword(s):  
Cell Migration ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Surface Membrane ◽  
Β1 Integrin ◽  
Cell Surface Membrane ◽  
Adhesion Sites ◽  
Endoplasmic Reticulum Protein ◽  
And Migration ◽  
Α5β1 Integrin

ABSTRACT Cytoskeleton-associated protein 4 (CKAP4) is an endoplasmic reticulum protein that is also present in the cell surface membrane, where it acts as a receptor for Dickkopf1 (DKK1). In this study, we found that CKAP4 interacts with β1 integrin and controls the recycling of α5β1 integrin independently of DKK1. In S2-CP8 cells, knockdown of CKAP4 but not DKK1 enlarged the size of cell adhesion sites and enhanced cell adhesion to fibronectin, resulting in decreased cell migration. When CKAP4 was depleted, the levels of α5 but not β1 integrin were increased in the cell surface membrane. A similar phenotype was observed in other cells expressing low levels of DKK1. In S2-CP8 cells, α5 integrin was trafficked with β1 integrin and CKAP4 to the lysosome or recycled with β1 integrin. In CKAP4-depleted cells, the internalization of α5β1 integrin was unchanged, but its recycling was upregulated. Knockdown of sorting nexin 17 (SNX17), a mediator of integrin recycling, abrogated the increased α5 integrin levels caused by CKAP4 knockdown. CKAP4 bound to SNX17, and its knockdown enhanced the recruitment of α5β1 integrin to SNX17. These results suggest that CKAP4 suppresses the recycling of α5β1 integrin and coordinates cell adhesion sites and migration independently of DKK1.

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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