Madhurima Singh
University of South Carolina
5 Papers
10 Citations
Madhurima Singh is an academic researcher from University of South Carolina. The author has contributed to research in topics: Protein kinase R & Pact. The author has an hindex of 5, co-authored 5 publications.
Chat about Author
Papers
TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.
Aïcha Daher,Ghislaine Laraki,Madhurima Singh,Carlos E Melendez-Peña,Sylvie Bannwarth,Antoine H.F.M. Peters,Eliane F. Meurs,Robert E. Braun,Rekha C. Patel,Anne Gatignol +9 more
TL;DR: It is demonstrated that in cells, TRBP controls PACT activation of PKR, an activity that is reversed by stress, demonstrating the relevance of this control in a physiological context.
138
Stress-induced phosphorylation of PACT reduces its interaction with TRBP and leads to PKR activation.
TL;DR: It is demonstrated for the first time that stress-induced PACT phosphorylation functions to free PACT from the inhibitory interaction with TRBP and also to enhance its interaction with PKR.
74
Increased interaction between PACT molecules in response to stress signals is required for PKR activation.
Madhurima Singh,Rekha C. Patel +1 more
TL;DR: It is demonstrated that PACT–PACT interaction is essential for efficient PKR activation, and enhanced interaction between PACT molecules when PACT is phosphorylated in response to stress signals on serines 246 and 287 is essential.
56
Essential role of PACT-mediated PKR activation in tunicamycin-induced apoptosis.
TL;DR: Reconstitution of PKR and PACT expression in the null cells renders them sensitive to tunicamycin, thus demonstrating that PACT-induced PKR activation plays an essential function in induction of apoptosis.
48
Contribution of the two dsRBM motifs to the double-stranded RNA binding and protein interactions of PACT.
TL;DR: Evaluated mutations within PACT's two evolutionarily conserved dsRBMs show that the two motifs contribute to varying extents in dsRNA binding, and protein interactions, and indicate that although the dsRBM motifs have high sequence conservation, their functional contribution in the context of the whole proteins needs to be determined by mutational analysis.
14