Chaudhary, Surbhi and Dhiman, Asmita and Patidar, Anil and Malhotra, Himanshu and Talukdar, Sharmila and Dilawari, Rahul and Chaubey, Gaurav Kumar and Modanwal, Radheshyam and Raje, Chaaya Iyengar and Raje, Manoj (2021) Moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) modulates protein aggregation. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, 1867 (10).

Full text not available from this repository. (Request a copy)

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.

Item Type:	Article
Additional Information:	The Copyright of this article belongs to ELSEVIER
Uncontrolled Keywords:	GAPDHHuntingtin; PrionAggregate; Multifunctional protein; Protein misfolding;
Subjects:	Q Science > QR Microbiology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	28 Mar 2022 11:48
Last Modified:	28 Mar 2022 11:48
URI:	http://crdd.osdd.net/open/id/eprint/2751

Actions (login required)

View Item