{Reference Type}: Journal Article
{Title}: A molecular switch controls assembly of bacterial focal adhesions.
{Author}: Attia B;My L;Castaing JP;Dinet C;Le Guenno H;Schmidt V;Espinosa L;Anantharaman V;Aravind L;Sebban-Kreuzer C;Nouailler M;Bornet O;Viollier P;Elantak L;Mignot T;
{Journal}: Sci Adv
{Volume}: 10
{Issue}: 22
{Year}: 2024 May 31
{Factor}: 14.957
{DOI}: 10.1126/sciadv.adn2789
{Abstract}: 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.