Scientific article
Open access

A molecular switch controls assembly of bacterial focal adhesions

Published inScience advances, vol. 10, no. 22, eadn2789
Publication date2024-05-31
First online date2024-05-29

Cell motility universally relies on spatial regulation of focal adhesion complexes (FAs) connecting the substrate to cellular motors. In bacterial FAs, the Adventurous gliding motility machinery (Agl-Glt) assembles at the leading cell pole following a Mutual gliding-motility protein (MglA)-guanosine 5'-triphosphate (GTP) gradient along the cell axis. Here, we show that GltJ, a machinery membrane protein, contains cytosolic motifs binding MglA-GTP and AglZ and recruiting the MreB cytoskeleton to initiate movement toward the lagging cell pole. In addition, MglA-GTP binding triggers a conformational shift in an adjacent GltJ zinc-finger domain, facilitating MglB recruitment near the lagging pole. This prompts GTP hydrolysis by MglA, leading to complex disassembly. The GltJ switch thus serves as a sensor for the MglA-GTP gradient, controlling FA activity spatially.

  • Focal Adhesions / metabolism
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / chemistry
  • Guanosine Triphosphate / metabolism
  • Protein Binding
Citation (ISO format)
ATTIA, Bouchra et al. A molecular switch controls assembly of bacterial focal adhesions. In: Science advances, 2024, vol. 10, n° 22, p. eadn2789. doi: 10.1126/sciadv.adn2789
Main files (1)
Article (Published version)
ISSN of the journal2375-2548

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