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Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation.

Abstract：

:Spinocerebellar ataxia type 5 (SCA5) is a neurodegenerative disease caused by mutations in the cytoskeletal protein β-III-spectrin. Previously, a SCA5 mutation resulting in a leucine-to-proline substitution (L253P) in the actin-binding domain (ABD) was shown to cause a 1000-fold increase in actin-binding affinity. However, the structural basis for this increase is unknown. Here, we report a 6.9 Å cryo-EM structure of F-actin complexed with the L253P ABD. This structure, along with co-sedimentation and pulsed-EPR measurements, demonstrates that high-affinity binding caused by the CH2-localized mutation is due to opening of the two CH domains. This enables CH1 to bind actin aided by an unstructured N-terminal region that becomes α-helical upon binding. This helix is required for association with actin as truncation eliminates binding. Collectively, these results shed light on the mechanism by which β-III-spectrin, and likely similar actin-binding proteins, interact with actin, and how this mechanism can be perturbed to cause disease.

journal_name

Nat Commun

journal_title

Nature communications

authors

Avery AW,Fealey ME,Wang F,Orlova A,Thompson AR,Thomas DD,Hays TS,Egelman EH

doi

10.1038/s41467-017-01367-w

subject

Has Abstract

pub_date

2017-11-07 00:00:00

pages

1350

issue

1

issn

2041-1723

pii

10.1038/s41467-017-01367-w

journal_volume

8

pub_type

杂志文章

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