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Proteinase K digestion of Annexin A11 fibrils

ABSTRACT: Human Annexin A11 (Uniprot accession no. P50995) head domain (residues 2-196) was recombinantly expressed, purified, fibrilized, and digested by proteinase K. Products were analyzed by LC/MS/MS.

INSTRUMENT(S): LTQ XL

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Lalit Deshmukh

PROVIDER: MSV000091107 | MassIVE | Fri Jan 20 16:56:00 GMT 2023

REPOSITORIES: MassIVE

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Publications

ALS Variants of Annexin A11's Proline-Rich Domain Impair Its S100A6-Mediated Fibril Dissolution.

Shihora Aman A Elias Ruben D RD Hammond John A JA Ghirlando Rodolfo R Deshmukh Lalit L

ACS chemical neuroscience 20230711 15

Mutations in the proline-rich domain (PRD) of annexin A11 are linked to amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease, and generate abundant neuronal A11 inclusions by an unknown mechanism. Here, we demonstrate that recombinant A11-PRD and its ALS-associated variants form liquidlike condensates that transform into β-sheet-rich amyloid fibrils. Surprisingly, these fibrils dissolved in the presence of S100A6, an A11 binding partner overexpressed in ALS. The ALS variants of ...[more]

PMID: 37433222

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