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© Sandrine Etienne-Manneville
Photo prise à l'avant (dans la protrusion) d'astrocytes primaires de rat en migration. Marquage par immunofluorescence montrant en rouge, p150 Glued, une protéine associée aux extrémités 'plus' des microtubules et en vert la tubuline des microtubules. La photographie montre l'accumulation de p150 Glued à l'avant des cellules en migration, où la protéine pourrait participer à l'ancrage des microtubules à la membrane plasmique. Pour essayer de corriger, les dérèglements observés lors de la migration des cellules d'astrocytes tumuraux ou gliomes on cherche à connaitre les mécanismes moléculaires fondamentaux qui controlent la polarisation et la migration cellulaires.
Publication : Biochemistry

Calmodulin-induced conformational and hydrodynamic changes in the catalytic domain of Bordetella pertussis adenylate cyclase toxin

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemistry - 19 Jan 2010

Karst JC, Sotomayor Pérez AC, Guijarro JI, Raynal B, Chenal A, Ladant D

Link to Pubmed [PMID] – 20000337

Biochemistry 2010 Jan;49(2):318-28

Bordetella pertussis, the causative agent of whooping cough, secretes among various toxins an adenylate cyclase (CyaA) that displays a unique mechanism of cell invasion, which involves a direct translocation of its N-terminal catalytic domain (AC, 400 residues) across the plasma membrane of the eukaryotic targeted cells. Once into the cytosol, AC is activated by endogenous calmodulin and produces toxic amounts of cAMP. The structure of AC in complex with the C-terminal part of calmodulin has recently been determined. However, as the structure of the catalytic domain in the absence of calmodulin is still lacking, the molecular basis of AC activation by calmodulin remains largely unknown. To characterize this activation mechanism, we investigated here the biophysical properties of the isolated catalytic domain in solution with or without calmodulin. We found that calmodulin triggered only minor modifications of the protein secondary and tertiary structure but had a pronounced effect on the hydrodynamic properties of AC. Indeed, while the isolated catalytic domain was spherical and hydrated, it underwent a significant elongation as well as compaction and dehydration upon calmodulin interaction. On the basis of these data, we propose a model for the structural transition between the calmodulin-free and calmodulin-bound AC.

https://www.ncbi.nlm.nih.gov/pubmed/20000337