Moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) modulates protein aggregation

Surbhi Chaudhary, Asmita Dhiman, Anil Patidar, Himanshu Malhotra, Sharmila Talukdar, Rahul Dilawari, Gaurav Kumar Chaubey, Radheshyam Modanwal, Chaaya Iyengar Raje, Manoj Raje

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

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 languageEnglish (US)
Article number166202
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Volume1867
Issue number10
DOIs
StatePublished - Oct 1 2021
Externally publishedYes

Keywords

  • Aggregate
  • GAPDH
  • Huntingtin
  • Multifunctional protein
  • Prion
  • Protein misfolding

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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