Mutations in actin used for structural studies partially disrupt β-thymosin/WH2 domains interaction. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue FEBS Letters Année : 2016

Mutations in actin used for structural studies partially disrupt β-thymosin/WH2 domains interaction.

Résumé

Understanding the structural basis of actin cytoskeleton remodeling requires stabilization of actin monomers, oligomers, and filaments in complex with partner proteins, using various biochemical strategies. Here, we report a dramatic destabilization of the dynamic interaction with a model β-thymosin/WH2 domain induced by mutations in actin. This result underlines that mutant actins should be used with prudence to characterize interactions with intrinsically disordered partners as destabilization of dynamic interactions, although identifiable by NMR, may be invisible to other structural techniques. It also highlights how both β-thymosin/WH2 domains and actin tune local structure and dynamics in regulatory processes involving intrinsically disordered domains.

Dates et versions

hal-01451650 , version 1 (01-02-2017)

Identifiants

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Célia Deville, Christine Girard-Blanc, Nadine Assrir, Naïma Nhiri, Eric Jacquet, et al.. Mutations in actin used for structural studies partially disrupt β-thymosin/WH2 domains interaction.. FEBS Letters, 2016, 590 (20), pp.3690-3699. ⟨10.1002/1873-3468.12423⟩. ⟨hal-01451650⟩
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