STXBP1 forms amyloid-like aggregates in rat brain and demonstrates amyloid properties in bacterial expression system

Prion. 2021 Dec;15(1):29-36. doi: 10.1080/19336896.2021.1883980.

Abstract

Amyloids are the fibrillar protein aggregates with cross-β structure. Traditionally amyloids were associated with pathology, however, nowadays more data is emerging about functional amyloids playing essential roles in cellular processes. We conducted screening for functional amyloids in rat brain. One of the identified proteins was STXBP1 taking part in vesicular transport and neurotransmitter secretion. Using SDD-AGE and protein fractionation we found out that STXBP1 forms small detergent-insoluble aggregates in rat brain. With immunoprecipitation analysis and C-DAG system, we showed that STXBP1 forms amyloid-like fibrils. Thus, STXBP1 demonstrates amyloid properties in rat brain and in bacterial expression system.

Keywords: Munc18-1; Proteomic screening; SNARE; STXBP1; amyloid; brain; functional amyloid; rat.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid* / metabolism
  • Amyloidosis*
  • Animals
  • Brain / metabolism
  • Munc18 Proteins / metabolism*
  • Rats

Substances

  • Amyloid
  • Munc18 Proteins
  • Stxbp1 protein, rat

Grants and funding

The reported study was funded by RFBR according to the research project #18-34-00419 to V.A.S., and SpbSU grants ID 73024371 and ID 73023210. Immunoprecipitation analysis was supported by RSF #16-16-10043 to M.E.V. and TEM was supported by RSF #20-14-00148 to J.V.S.