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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 : The Journal of biological chemistry

The extreme C terminus of the effector ExoY is crucial for binding to its eukaryotic activator, F-actin

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 30 Oct 2018

Belyy A, Santecchia I, Renault L, Bourigault B, Ladant D, Mechold U

Link to Pubmed [PMID] – 30377256

J. Biol. Chem. 2018 12;293(51):19785-19796

Bacterial nucleotidyl cyclase toxins are potent virulence factors that upon entry into eukaryotic cells are stimulated by endogenous cofactors to catalyze the production of large amounts of 3’5′-cyclic nucleoside monophosphates. The activity of the effector ExoY from is stimulated by the filamentous form of actin (F-actin). Utilizing yeast phenotype analysis, site-directed mutagenesis, functional biochemical assays, and confocal microscopy, we demonstrate that the last nine amino acids of the C terminus of ExoY are crucial for the interaction with F-actin and, consequently, for ExoY’s enzymatic activity and toxicity in a yeast model. We observed that isolated C-terminal sequences of ExoY that had been fused to a carrier protein bind to F-actin and that synthetic peptides corresponding to the extreme ExoY C terminus inhibit ExoY enzymatic activity and compete with the full-length enzyme for F-actin binding. Interestingly, we noted that various isolates of the PA14 family, including highly virulent strains, harbor ExoY variants with a mutation altering the C terminus of this effector. We found that these naturally occurring ExoY variants display drastically reduced enzymatic activity and toxicity. Our findings shed light on the molecular basis of the ExoY-F-actin interaction, revealing that the extreme C terminus of ExoY is critical for binding to F-actin in target cells and that some isolates carry C-terminally mutated, low-activity ExoY variants.

https://www.ncbi.nlm.nih.gov/pubmed/30377256