%0 Journal Article
%T A molecular switch controls assembly of bacterial focal adhesions.
%A Attia B
%A My L
%A Castaing JP
%A Dinet C
%A Le Guenno H
%A Schmidt V
%A Espinosa L
%A Anantharaman V
%A Aravind L
%A Sebban-Kreuzer C
%A Nouailler M
%A Bornet O
%A Viollier P
%A Elantak L
%A Mignot T
%J Sci Adv
%V 10
%N 22
%D 2024 May 31
%M 38809974
%F 14.957
%R 10.1126/sciadv.adn2789
%X 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.