Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope - I2BC Accéder directement au contenu
Article Dans Une Revue Structure (London, England: 1993) Année : 2016

Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope

Résumé

Arpin is a newly discovered regulator of actin polymerization at the cell leading edge, which steers cell migration by exerting a negative control on the Arp2/3 complex. Arpin proteins have an acidic tail homologous to the acidic motif of the VCA domain of nucleation-promoting factors (NPFs). This tail is predicted to compete with the VCA of NPFs for binding to the Arp2/3 complex, thereby mitigating activation and/or tethering of the complex to sites of actin branching. Here, we investigated the structure of full-length Arpin using synchrotron small-angle X-ray scattering, and of its acidic tail in complex with an ankyrin repeats domain using X-ray crystallography. The data were combined in a hybrid model in which the acidic tail extends from the globular core as a linear peptide and forms a primary epitope that is readily accessible in unbound Arpin and suffices to tether Arpin to interacting proteins with high affinity.

Dates et versions

hal-02393770 , version 1 (04-12-2019)

Identifiants

Citer

Susan Fetics, Aurélien Thureau, Valérie Campanacci, Magali Aumont-Nicaise, Irène Dang, et al.. Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure (London, England: 1993), 2016, 24 (2), pp.252--260. ⟨10.1016/j.str.2015.12.001⟩. ⟨hal-02393770⟩
13 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More