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

doi:10.1016/j.bbadis.2021.166202

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 journal › Article › peer-review

6 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 language	English (US)
Article number	166202
Journal	Biochimica et Biophysica Acta - Molecular Basis of Disease
Volume	1867
Issue number	10
DOIs	https://doi.org/10.1016/j.bbadis.2021.166202
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

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10.1016/j.bbadis.2021.166202

Cite this

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title = "Moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) modulates protein aggregation",

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.",

keywords = "Aggregate, GAPDH, Huntingtin, Multifunctional protein, Prion, Protein misfolding",

author = "Surbhi Chaudhary and Asmita Dhiman and Anil Patidar and Himanshu Malhotra and Sharmila Talukdar and Rahul Dilawari and Chaubey, {Gaurav Kumar} and Radheshyam Modanwal and Raje, {Chaaya Iyengar} and Manoj Raje",

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doi = "10.1016/j.bbadis.2021.166202",

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AU - Chaudhary, Surbhi

AU - Dhiman, Asmita

AU - Patidar, Anil

AU - Malhotra, Himanshu

AU - Talukdar, Sharmila

AU - Dilawari, Rahul

AU - Chaubey, Gaurav Kumar

AU - Modanwal, Radheshyam

AU - Raje, Chaaya Iyengar

AU - Raje, Manoj

PY - 2021/10/1

Y1 - 2021/10/1

N2 - 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.

AB - 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.

KW - Aggregate

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KW - Huntingtin

KW - Multifunctional protein

KW - Prion

KW - Protein misfolding

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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