Birkbeck College, London
"A molecular switch controls assembly of bacterial focal adhesions"
Science Advances 10.1126/sciadv.adn2789
Attia, B., My, L., Castaing, J. P., Dinet, C., Le Guenno, H., Schmidt, V., Espinosa, L., Anantharaman, V., Aravind, L., Sebban-Kreuzer, C., Nouailler, M., Bornet, O., Viollier, P., Elantak, L., and Mignot, T.
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Bouchra Attia (30 years old) began her academic journey with a Bachelor's degree in Biochemistry, Chemistry, and Biopharmaceutics at Aix-Marseille University, followed by a Master's degree in Bioinformatics, Structural Biochemistry, and Genomics. During her PhD (defended in 2022), she explored the fascinating world of bacterial motility under the supervision of Dr. Latifa Elantak at the CNRS-LISM laboratory in Marseille in collaboration with Dr. Tâm Mignot. Her research focused on the structure and role of the GltJ protein, a key player in regulating a specific type of bacterial movement called "adventurous motility." In 2023, she undertook a short postdoctoral position in the same CNRS-LISM laboratory, under the supervision of Dr. Latifa Elantak and Dr. Romain Mercier. Her research project aimed to decipher the molecular mechanism behind the activation of type IVa pili, crucial for twitching motility.
Currently, she is a postdoctoral researcher at Birkbeck College in London, under the supervision of Prof. Carolyn A. Moores. Her new project focuses on the Arp2/3 complex, a critical regulator of actin dynamics in cells, to elucidate how structural variations within this complex influence cell migration and muscle fiber development.
Contact
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Article Summary:
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. Combining NMR spectroscopy for structure and interaction studies to motility assays and FAs dynamics monitored by TIRF microscopy, we identified that MglA-GTP binding triggers a conformational shift in an adjacent GltJ zinc-finger domain, facilitating MglB recruitment near the lagging pole. Thus, GltJ acts as a molecular switch that prompts GTP hydrolysis by MglA, leading to complex disassembly. The GltJ protein emerges as a new class of molecular switches that act in concert with GTPases to control FA activity spatially.
