2014
DOI: 10.1091/mbc.e13-03-0162
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New single-molecule speckle microscopy reveals modification of the retrograde actin flow by focal adhesions at nanometer scales

Abstract: This paper introduces a new, easy-to-use method of fluorescence single-molecule speckle microscopy for actin with nanometer-scale accuracy. This new method reveals that actin flows in front of mature focal adhesions (FAs) are fast and biased toward FAs, suggesting that mature FAs are actively engaged in pulling and remodeling the local actin network.

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Cited by 46 publications
(170 citation statements)
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“…The barbed end depolymerization rate is increased ~3-fold by twinfilin, whereas in combination with Srv2/CAP, pointed end depolymerization increases an additional 17-fold 139 . Interestingly, different F-actin networks disassemble at different rates, which influences the recycling of G-actin 140 . For example, in XTC fibroblasts, the majority of F-actin in stress fibers disassembles five times slower than in other fibers, whereas F-actin in filopodia disassembles 2.4 times slower than in lamellipodia 140 .…”
Section: Figurementioning
confidence: 99%
See 1 more Smart Citation
“…The barbed end depolymerization rate is increased ~3-fold by twinfilin, whereas in combination with Srv2/CAP, pointed end depolymerization increases an additional 17-fold 139 . Interestingly, different F-actin networks disassemble at different rates, which influences the recycling of G-actin 140 . For example, in XTC fibroblasts, the majority of F-actin in stress fibers disassembles five times slower than in other fibers, whereas F-actin in filopodia disassembles 2.4 times slower than in lamellipodia 140 .…”
Section: Figurementioning
confidence: 99%
“…Interestingly, different F-actin networks disassemble at different rates, which influences the recycling of G-actin 140 . For example, in XTC fibroblasts, the majority of F-actin in stress fibers disassembles five times slower than in other fibers, whereas F-actin in filopodia disassembles 2.4 times slower than in lamellipodia 140 . The coordinated actions of these diverse disassembly factors allow for rapid actin disassembly, replenishing the G-actin pool for subsequent network assembly (Figure 2).…”
Section: Figurementioning
confidence: 99%
“…Stresses generated within the cytoskeleton drive the rearward movement of actin known as retrograde flow. Engagement of focal adhesions results in a reduction of actin retrograde flow rates around adhesion sites [4648] and an increase in traction stresses [27] and thereby can be thought of as a ‘molecular clutch’ [49,50]. The ‘clutch engagement’ at a focal adhesion involves increases in density and affinity of binding interactions spanning the actin cytoskeleton and the ECM.…”
Section: Force Transmission At Focal Adhesionsmentioning
confidence: 99%
“…Filopodial protrusions extend against retrograde actin flow in the steady state (Yamashiro et al, 2014). Many of the cellular protrusions involved in cell migration are formed transiently and disappear subsequently.…”
Section: Discussionmentioning
confidence: 99%