Cyclic stretch induces reorientation of cells in a Src family kinase- and p130Cas-dependent manner.

Recognition of external mechanical signals by cells is an essential process for life. One important mechanical signal experienced by various cell types, e.g.

Substrate, focal adhesions, and actin filaments: a mechanical unit with a weak spot for mechanosensitive proteins.

Mechanosensing is a vital prerequisite for dynamic remodeling of focal adhesions and cytoskeletal structures upon substrate deformation. For example, tissue formation, directed cell orientation or cell differentiation are regulated by such mechanosensing processes. Focal adhesions and the actin cytoskeleton are believed to be involved in these processes, but where mechanosensing molecules are located and how elastic substrate, focal adhesions and the cytoskeleton couple with each other upon substrate deformation still remains obscure.

Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions.

Focal adhesions (FAs) connect the cellular actin cytoskeleton via integrin with the extracellular matrix. They comprise of many structural and signaling proteins which are highly dynamic, well regulated, and responsible for the sensing of physical properties from the environment. Vinculin is a protein that incorporates all these functions.

The key feature for early migratory processes: Dependence of adhesion, actin bundles, force generation and transmission on filopodia.

Migration of cells is one of the most essential prerequisites to form higher organisms and depends on a strongly coordinated sequence of processes. Early migratory events include substrate sensing, adhesion formation, actin bundle assembly and force generation. While substrate sensing was ascribed to filopodia, all other processes were believed to depend mainly on lamellipodia of migrating cells.

Becoming stable and strong: the interplay between vinculin exchange dynamics and adhesion strength during adhesion site maturation.

The coordinated formation and release of focal adhesions is necessary for cell attachment and migration. According to current models, these processes are caused by temporal variations in protein composition. Protein incorporation into focal adhesions is believed to be controlled by phosphorylation.

Presenilin 1 affects focal adhesion site formation and cell force generation via c-Src transcriptional and posttranslational regulation.

Presenilin 1 and 2 (PS) are critical components of the gamma-secretase complex that cleaves type I transmembrane proteins within their transmembrane domains. This process leads to release of proteolytically processed products from cellular membranes and plays an essential role in signal transduction or vital functions as cell adhesion. Here we studied the function of presenilins in cell-matrix interaction of wild-type and PS knock-out mouse embryonic fibroblasts.

One step ahead: role of filopodia in adhesion formation during cell migration of keratinocytes.

Cell adhesion is an essential prerequisite for cell function and movement. It depends strongly on focal adhesion complexes connecting the extracellular matrix to the actin cytoskeleton. Especially in moving cells focal adhesions are highly dynamic and believed to be formed closely behind the leading edge.