scholarly journals The mechanism of force transmission at bacterial focal adhesion complexes

Nature ◽  
2016 ◽  
Vol 539 (7630) ◽  
pp. 530-535 ◽  
Author(s):  
Laura M. Faure ◽  
Jean-Bernard Fiche ◽  
Leon Espinosa ◽  
Adrien Ducret ◽  
Vivek Anantharaman ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Force Transmission

Force-induced focal adhesion translocation: effects of force amplitude and frequency

2004 ◽  
Vol 287 (4) ◽  
pp. C954-C962 ◽  
Author(s):  
P. J. Mack ◽  
M. R. Kaazempur-Mofrad ◽  
H. Karcher ◽  
R. T. Lee ◽  
R. D. Kamm
Keyword(s):  
Tyrosine Kinase ◽  
Focal Adhesion ◽  
Magnetic Beads ◽  
Kinase Inhibitors ◽  
Kinase Inhibitor ◽  
Apical Cell ◽  
Force Transmission ◽  
Shear Forces ◽  
Apical Cell Membrane ◽  
Adhesion Sites

Vascular endothelial cells rapidly transduce local mechanical forces into biological signals through numerous processes including the activation of focal adhesion sites. To examine the mechanosensing capabilities of these adhesion sites, focal adhesion translocation was monitored over the course of 5 min with GFP-paxillin while applying nN-level magnetic trap shear forces to the cell apex via integrin-linked magnetic beads. A nongraded steady-load threshold for mechanotransduction was established between 0.90 and 1.45 nN. Activation was greatest near the point of forcing (<7.5 μm), indicating that shear forces imposed on the apical cell membrane transmit nonuniformly to the basal cell surface and that focal adhesion sites may function as individual mechanosensors responding to local levels of force. Results from a continuum, viscoelastic finite element model of magnetocytometry that represented experimental focal adhesion attachments provided support for a nonuniform force transmission to basal surface focal adhesion sites. To further understand the role of force transmission on focal adhesion activation and dynamics, sinusoidally varying forces were applied at 0.1, 1.0, 10, and 50 Hz with a 1.45 nN offset and a 2.25 nN maximum. At 10 and 50 Hz, focal adhesion activation did not vary with spatial location, as observed for steady loading, whereas the response was minimized at 1.0 Hz. Furthermore, applying the tyrosine kinase inhibitors genistein and PP2, a specific Src family kinase inhibitor, showed tyrosine kinase signaling has a role in force-induced translocation. These results highlight the mutual importance of force transmission and biochemical signaling in focal adhesion mechanotransduction.

scholarly journals Tension is required but not sufficient for focal adhesion maturation without a stress fiber template

2012 ◽  
Vol 196 (3) ◽  
pp. 363-374 ◽  
Author(s):  
Patrick W. Oakes ◽  
Yvonne Beckham ◽  
Jonathan Stricker ◽  
Margaret L. Gardel
Keyword(s):  
Focal Adhesion ◽  
Myosin Ii ◽  
Focal Adhesions ◽  
Stress Fiber ◽  
Matrix Remodeling ◽  
Force Transmission ◽  
Fiber Assembly ◽  
Wide Range ◽  
Structural Template

Focal adhesion composition and size are modulated in a myosin II–dependent maturation process that controls adhesion, migration, and matrix remodeling. As myosin II activity drives stress fiber assembly and enhanced tension at adhesions simultaneously, the extent to which adhesion maturation is driven by tension or altered actin architecture is unknown. We show that perturbations to formin and α-actinin 1 activity selectively inhibited stress fiber assembly at adhesions but retained a contractile lamella that generated large tension on adhesions. Despite relatively unperturbed adhesion dynamics and force transmission, impaired stress fiber assembly impeded focal adhesion compositional maturation and fibronectin remodeling. Finally, we show that compositional maturation of focal adhesions could occur even when myosin II–dependent cellular tension was reduced by 80%. We propose that stress fiber assembly at the adhesion site serves as a structural template that facilitates adhesion maturation over a wide range of tensions. This work identifies the essential role of lamellar actin architecture in adhesion maturation.

scholarly journals Correction: Talin tension sensor reveals novel features of focal adhesion force transmission and mechanosensitivity

2016 ◽  
Vol 214 (2) ◽  
pp. 231-231 ◽  
Author(s):  
Abhishek Kumar ◽  
Mingxing Ouyang ◽  
Koen Van den Dries ◽  
Ewan James McGhee ◽  
Keiichiro Tanaka ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Adhesion Force ◽  
Force Transmission ◽  
Tension Sensor

scholarly journals Actin flow-dependent and -independent force transmission through integrins

2020 ◽  
Vol 117 (51) ◽  
pp. 32413-32422
Author(s):  
Tristan P. Driscoll ◽  
Sang Joon Ahn ◽  
Billy Huang ◽  
Abhishek Kumar ◽  
Martin A. Schwartz
Keyword(s):  
Binding Site ◽  
Focal Adhesion ◽  
Protein Interactions ◽  
Flow Speed ◽  
Substrate Stiffness ◽  
Actin Binding ◽  
Force Transmission ◽  
Force Transfer ◽  
Independent Mechanism ◽  
Actin Binding Site

Integrin-dependent adhesions mediate reciprocal exchange of force and information between the cell and the extracellular matrix. These effects are attributed to the “focal adhesion clutch,” in which moving actin filaments transmit force to integrins via dynamic protein interactions. To elucidate these processes, we measured force on talin together with actin flow speed. While force on talin in small lamellipodial adhesions correlated with actin flow, talin tension in large adhesions further from the cell edge was mainly flow-independent. Stiff substrates shifted force transfer toward the flow-independent mechanism. Flow-dependent force transfer required talin’s C-terminal actin binding site, ABS3, but not vinculin. Flow-independent force transfer initially required vinculin and at later times the central actin binding site, ABS2. Force transfer through integrins thus occurs not through a continuous clutch but through a series of discrete states mediated by distinct protein interactions, with their ratio modulated by substrate stiffness.

scholarly journals Nanopatterning reveals an ECM area threshold for focal adhesion assembly and force transmission that is regulated by integrin activation and cytoskeleton tension

2012 ◽  
Vol 125 (21) ◽  
pp. 5110-5123 ◽  
Author(s):  
S. R. Coyer ◽  
A. Singh ◽  
D. W. Dumbauld ◽  
D. A. Calderwood ◽  
S. W. Craig ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Force Transmission ◽  
Integrin Activation

scholarly journals Dystrophin modulates focal adhesion tension and YAP-mediated mechanotransduction

2021 ◽  
Author(s):  
Maria Paz Ramirez ◽  
Michael JM Anderson ◽  
Lauren J Sundby ◽  
Anthony R Hagerty ◽  
Sophia J Wenthe ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Muscular Dystrophy ◽  
Focal Adhesion ◽  
Adhesion Force ◽  
Muscle Protein ◽  
Focal Adhesions ◽  
Becker Muscular Dystrophy ◽  
Missense Mutations ◽  
Force Transmission ◽  
Cell Membrane Stability

Dystrophin is an essential muscle protein that contributes to cell membrane stability by linking the actin cytoskeleton to the extracellular matrix. The absence or impaired function of dystrophin causes muscular dystrophy. Focal adhesions are mechanosensitive adhesion complexes that also connect the cytoskeleton to the extracellular matrix. However, the interplay between dystrophin and focal adhesion force transmission has not been investigated. Using a bioluminescent tension sensor, we measured focal adhesion tension in transgenic C2C12 myoblasts expressing wild type (WT) dystrophin, a non-pathogenic SNP (I232M), or two missense mutations associated with Duchenne (L54R), or Becker muscular dystrophy (L172H). We found that myoblasts expressing WT or nonpathogenic I232M dystrophin showed increased focal adhesion tension compared to non-transgenic myoblasts, while myoblasts expressing L54R or L172H dystrophin presented with decreased focal adhesion tension. Moreover, myoblasts expressing L54R or L172H dystrophin showed decreased YAP activation and exhibited slower and less directional migration compared to cells expressing WT or I232M dystrophin. Our results suggest that disease-causing missense mutations in dystrophin may disrupt a cellular tension sensing pathway in dystrophic skeletal muscle.

Early signalling events of autophagy

2013 ◽  
Vol 55 ◽  
pp. 1-15 ◽  
Author(s):  
Laura E. Gallagher ◽  
Edmond Y.W. Chan
Keyword(s):  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Mammalian Cells ◽  
Mammalian Target Of Rapamycin ◽  
Interacting Protein ◽  
The Core ◽  
Autophagy Gene ◽  
Autophagy Induction ◽  
Cellular Pathways

Autophagy is a conserved cellular degradative process important for cellular homoeostasis and survival. An early committal step during the initiation of autophagy requires the actions of a protein kinase called ATG1 (autophagy gene 1). In mammalian cells, ATG1 is represented by ULK1 (uncoordinated-51-like kinase 1), which relies on its essential regulatory cofactors mATG13, FIP200 (focal adhesion kinase family-interacting protein 200 kDa) and ATG101. Much evidence indicates that mTORC1 [mechanistic (also known as mammalian) target of rapamycin complex 1] signals downstream to the ULK1 complex to negatively regulate autophagy. In this chapter, we discuss our understanding on how the mTORC1–ULK1 signalling axis drives the initial steps of autophagy induction. We conclude with a summary of our growing appreciation of the additional cellular pathways that interconnect with the core mTORC1–ULK1 signalling module.

111-OR: Pancreatic Elastase Regulates Human Beta-Cell Proliferation via the Focal Adhesion and PAR2 Signaling Pathways

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 111-OR
Author(s):  
GIORGIO BASILE ◽  
AMEDEO VETERE ◽  
KA-CHEUK LIU ◽  
JIANG HU ◽  
OLOV ANDERSSON ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Beta Cell ◽  
Signaling Pathways ◽  
Focal Adhesion ◽  
Beta Cell Proliferation ◽  
Pancreatic Elastase ◽  
Human Beta Cell
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