Related Experiment Video
Updated: Aug 19, 2026

Induction of Adhesion-dependent Signals Using Low-intensity Ultrasound
Published on: May 8, 2012
Emerging views on integrin signaling via Rac1 during invasin-promoted bacterial uptake
1Department of Molecular Biology and Microbiology, Howard Hughes Medical Institute, Tufts University School of Medicine, 150 Harrison Avenue, Boston, MA 02111, USA.
Abstract:
Enteropathogenic Yersinia species encode invasin, which promotes uptake into host cells by binding beta1 integrins. Invasin may cluster integrin heterodimers extracellularly and cause the integrin alpha and beta chains to splay apart in the cytoplasm. Cdc42 signaling is not essential for Yersinia uptake, whereas invasin crucially triggers Rac1-mediated signals that enable internalization. The signals linking invasin-mediated adhesion to Rac1 activation are not clear, but a novel kinase may release it from RhoGDI so that Rac1 can be activated, for example by Dock180. Rac1 may act via Arp2/3, phosphatidylinositol 4,5-bisphosphate and capping-proteins in the formation of nascent phagosomes during Yersinia uptake.
Related Concept Videos
Intracellular Signaling Affects Focal Adhesions
Some...
Activation of Integrins
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Cancer Cell Migration through Invadopodia
Integrins
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Mechanism of Lamellipodia Formation
Cell Polarization by Rho Proteins

