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

被引：5
|
作者：
Chaudhary, Surbhi [1 ]
Dhiman, Asmita [1 ]
Patidar, Anil [1 ]
Malhotra, Himanshu [1 ]
Talukdar, Sharmila [1 ]
Dilawari, Rahul [1 ]
Chaubey, Gaurav Kumar [1 ]
Modanwal, Radheshyam [1 ]
Raje, Chaaya Iyengar [2 ]
Raje, Manoj [1 ]
机构：
[1] CSIR, Inst Microbial Technol, Sect 39A, Chandigarh 160036, India
[2] Natl Inst Pharmaceut Educ & Res, Phase 10,Sect 67, Sas Nagar 160062, Punjab, India
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE | 2021年 / 1867卷 / 10期
关键词：
GAPDH; Huntingtin; Prion; Aggregate; Multifunctional protein; Protein misfolding; ALZHEIMERS-DISEASE; POLYGLUTAMINE; EXPANSIONS;
D O I：
10.1016/j.bbadis.2021.166202
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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页数：4
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