Imperial College London
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DrMarufAli

Faculty of Natural Sciences, Department of Life Sciences

Reader in Molecular and Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 5733maruf.ali Website

 
 
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Location

 

505Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Prischi:2014:10.1038/ncomms4554,
author = {Prischi, F and Nowak, PR and Carrara, M and Ali, MMU},
doi = {10.1038/ncomms4554},
journal = {Nat Commun},
title = {Phosphoregulation of Ire1 RNase splicing activity.},
url = {http://dx.doi.org/10.1038/ncomms4554},
volume = {5},
year = {2014}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Ire1 is activated in response to accumulation of misfolded proteins within the endoplasmic reticulum as part of the unfolded protein response (UPR). It is a unique enzyme, possessing both kinase and RNase activity that is required for specific splicing of Xbp1 mRNA leading to UPR activation. How phosphorylation impacts on the Ire1 splicing activity is unclear. In this study, we isolate distinct phosphorylated species of Ire1 and assess their effects on RNase splicing both in vitro and in vivo. We find that phosphorylation within the kinase activation loop significantly increases RNase splicing in vitro. Correspondingly, mutants of Ire1 that cannot be phosphorylated on the activation loop show decreased specific Xbp1 and promiscuous RNase splicing activity relative to wild-type Ire1 in cells. These data couple the kinase phosphorylation reaction to the activation state of the RNase, suggesting that phosphorylation of the activation loop is an important step in Ire1-mediated UPR activation.
AU  - Prischi,F
AU  - Nowak,PR
AU  - Carrara,M
AU  - Ali,MMU
DO  - 10.1038/ncomms4554
PY  - 2014///
TI  - Phosphoregulation of Ire1 RNase splicing activity.
T2  - Nat Commun
UR  - http://dx.doi.org/10.1038/ncomms4554
UR  - https://www.ncbi.nlm.nih.gov/pubmed/24704861
UR  - http://hdl.handle.net/10044/1/13817
VL  - 5
ER  -
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