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DTSTAMP:20260424T143502Z
UID:1683536400@ist.ac.at
DTSTART:20230508T110000
DTEND:20230508T120000
DESCRIPTION:Speaker: Bouchra Attia\nhosted by Florian Schur\nAbstract: Cell
  motility is central to all biological systems\, from bacteria to animals\
 , allowing adaptative responses and multicellular development. In the bact
 erium Myxococcus xanthus\, single cells glide using the adventurous motili
 ty allowing them to explore new places and invade prey colonies. This moti
 lity is dependent on the assembly of bacterial focal adhesion complexes (b
 FAs) which are macromolecular machines linking the intracellular cytoskel
 eton to the extracellular substrate. bFAs are composed of (i) a cytoplasm
 ic platform consisting of the MglA-GTP and AglZ proteins\, (ii) a molecula
 r motor (Agl) energizing (iii) a multiprotein Glt complex (GltA to GltK) c
 rossing the entire bacterial membrane.bFA assembles at the leading pole of
  the cell and moves in the direction of the lagging cell pole\, attaching 
 to the substrate thus powering the cell directional movement. To date\, th
 ere is no structural exploration of protein interactions in the Agl-Glt sy
 stem that would provide a molecular understanding of Glt proteins function
  in this motility system.Here\, we show that the transmembrane GltJ protei
 n contains two cytosolic motifs (ZnR and GYF domains) that link the motili
 ty machinery to the cytoplasmic platform.By combining NMR spectroscopy for
  structure and interaction studies with motility assays and bFAs dynamics 
 by TIRF microscopy\, we identified that GltJ drives bFAs assembly by indep
 endently recruiting MglA-GTP (Linker) and AglZ (GYF). Remarkably\, binding
  of MglA-GTP causes a switch in the conformation of an adjacent Zinc finge
 r domain (ZnR) that becomes available to recruit MglB\, a MglA GTPase-Acti
 vating Protein. This binding activates GTP hydrolysis\, which dissociates 
 MglA from GltJ thus triggering bFAs disassembly in vivo.GltJ protein thus 
 emerges as a new class of molecular switches which act in concert with GTP
 ases to control bFAs dynamics.
LOCATION:Big Seminar Room B / Sunstone Building\, Ground Floor\, ISTA
ORGANIZER:
SUMMARY:Bouchra Attia: A novel molecular switch controls assembly and regul
 ation of bacterial focal adhesions
URL:https://talks-calendar.ista.ac.at/events/4139
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