Phosphorylation of α‑Synuclein Fibrils at S129 Changes DNAJB1 Binding as Probed by Solid-State NMR.

ABSTRACT: Amyloid fibrils formed by the protein α-synuclein are implicated in the pathogenesis of synucleinopathies. In addition to their rigid cross-β core, these fibrils have intrinsically disordered regions on their surface, which are important for interactions with other cellular components, such as chaperones. Chaperones play a vital role in preventing and reversing amyloid formation in neurodegenerative diseases. How they recognize misfolded proteins is an active field of research. DNAJB1 is a cochaperone that recognizes fibrils and recruits other chaperones such as Hsp70 and Apg2, which collectively disaggregate fibrils formed by α-synuclein, tau, and huntingtin. Because DNAJB1 was reported to bind the C-terminus of α-synuclein and S129 in this C-terminus is predominantly phosphorylated in pa

SUBMITTER: Pacheco S 

PROVIDER: S-EPMC12848675 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature