Abstract
Onset of protein aggregation reflects failure of the cellular folding machinery to keep aggregation-prone protein from misfolding and accumulating into a non-degradable state. FRET based analysis and biochemical data reveal that cytosolic prion (cyPrP) and httQ-103 interact with the multifunctional protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) leading to few detectable aggregates in GAPDH-over expressing cells.The preventive effect of GAPDH suggests that this abundant and long-lived cytoplasmic protein has an active role in the shielding and maintenance, in soluble form of proteins as heterogeneous as huntingtin and cyPrP.
Original language | English (US) |
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Article number | 166202 |
Journal | Biochimica et Biophysica Acta - Molecular Basis of Disease |
Volume | 1867 |
Issue number | 10 |
DOIs | |
State | Published - Oct 1 2021 |
Externally published | Yes |
Keywords
- Aggregate
- GAPDH
- Huntingtin
- Multifunctional protein
- Prion
- Protein misfolding
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology