TY - JOUR
T1 - Moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) modulates protein aggregation
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
N1 - Funding Information:
Mr. Anil Theophilus & Mr. Randeep Sharma are acknowledged for technical assistance. S.C., H.M. and R.S.M. received fellowships from University Grants Commission India , A.D., A.P., G.K.C. and S.T. from Department of Biotechnology , India and R.D. was supported by a fellowship of the Indian Council of Medical Research . Award of a Senior Research Associateship to M.R. by NRC, USA is acknowledged. Financial support of CSIR , DBT and DST is acknowledged. This is IMTECH communication No. 083/2016.
Funding Information:
Mr. Anil Theophilus & Mr. Randeep Sharma are acknowledged for technical assistance. S.C. H.M. and R.S.M. received fellowships from University Grants Commission India, A.D. A.P. G.K.C. and S.T. from Department of Biotechnology, India and R.D. was supported by a fellowship of the Indian Council of Medical Research. Award of a Senior Research Associateship to M.R. by NRC, USA is acknowledged. Financial support of CSIR, DBT and DST is acknowledged. This is IMTECH communication No. 083/2016.
Publisher Copyright:
© 2021 Elsevier B.V.
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
KW - GAPDH
KW - Huntingtin
KW - Multifunctional protein
KW - Prion
KW - Protein misfolding
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U2 - 10.1016/j.bbadis.2021.166202
DO - 10.1016/j.bbadis.2021.166202
M3 - Article
C2 - 34144092
AN - SCOPUS:85110234702
SN - 0925-4439
VL - 1867
JO - Biochimica et Biophysica Acta - Molecular Basis of Disease
JF - Biochimica et Biophysica Acta - Molecular Basis of Disease
IS - 10
M1 - 166202
ER -