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.

引用

页数：4

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