PhD student at TU Delft, Netherlands. Dogterom & Koenderink labs. I am from Paris, France.

Vincent Louis | Linktree

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In this work, produced by the laboratory of one of the pioneers in the field of integrins, the authors discuss the inside-out and outside-in models of integrin activation and propose a mixed model based on a primo-traction by actin.

The integrin, a smart molecular clamp

The authors are interested in the force-independent activation of talin by charged lipids that trigger a shift from a globular, inactive conformation, to an open extended one.

Force-independent activation of talin by charged lipids

The authors present how stretchable proteins such as talin reveal their binding domains when sufficient force is applied.

Force-dependent activation of talin by stretching

ABS3 is hypothesized to be the initial site to engage actin and allow the application of mechanical force across the talin molecule causing it to stretch and reveal cryptic protein binding sites.

Stretching of talin by actin from its C-terminal actin-binding site 3 (ABS3)

The Formation of Focal Adhesions, in video

In this work, the authors express only the transmembrane and cytosolic portions of the alpha and beta subunits of an integrin in E. coli.

How a truncated integrin can be expressed in E. coli

The pioneers in transmembrane protein reconstitution present the essentials of the technique. A reference for all experimenters.

The recipe to make proteoliposomes 

The authors review the plethora of adaptations of supported lipid bilayers, including protein tethered-supported lipid bilayers, that allow to attach the protein to resist force assays, and to control their orientation.

Protein-tethered supported lipid bilayers

The authors anchor a transmembrane protein to a PEG cushion using a histidine tag in order to stretch it with AFM. They also show how PEG-tethered lipids can aid in the formation of the bilayer.

Oriented membrane protein reconstitution under AFM

The ABS3 of talin forms a catch bond with F-actin when force is applied toward the pointed end of the actin filament, with binding lifetimes >100-fold longer than when force is applied toward the barbed end.

A look at talin's ABS3 with an optical trap

In GUVs, the authors simultaneously encapsulate integrin, talin, and another of its partners, and actin. The forces are not exerted directly on the GUV, but rather internally through the introduction of actomyosin.

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All encapsulated in a GUV

M. Dogterom Lab - TU Delft

G. Koenderink Lab - TU Delft

Vincent Louis

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Vincent Louis

PhD student at TU Delft, Netherlands. Dogterom & Koenderink labs. I am from Paris, France.

Want to keep a souvenir?

References in this poster

The laboratories

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