Imperial College London
Alternate

DrWengangChai

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Senior Research Fellow
 
 
 
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Contact

 

+44 (0)20 7594 2596w.chai

 
 
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Location

 

Burlington DanesHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Wang:2012:10.1371/journal.pone.0037427,
author = {Wang, S and Huang, X and Sun, D and Xin, X and Pan, Q and Peng, S and Liang, Z and Luo, C and Yang, Y and Jiang, H and Huang, M and Chai, W and Ding, J and Geng, M},
doi = {10.1371/journal.pone.0037427},
journal = {PLoS ONE},
title = {Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling},
url = {http://dx.doi.org/10.1371/journal.pone.0037427},
volume = {7},
year = {2012}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two importanttypes of post-translational modifications, often occur on the same protein and bear a reciprocal relationship. In additionto the well documented phosphorylations that control Akt activity, Akt also undergoes O-GlcNAcylation, but the interplaybetween these two modifications and the biological significance remain unclear, largely due to the technique challenges.Here, we applied a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent Ophosphateimmunodetection. Such an easy method enabled us to visualize endogenous glycosylated andphosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on itsphosphorylation. Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylationsat Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressedcell proliferation and migration capabilities. Together, this study revealed an extensive crosstalk between OGlcNAcylationsand phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification forAkt signaling.
AU  - Wang,S
AU  - Huang,X
AU  - Sun,D
AU  - Xin,X
AU  - Pan,Q
AU  - Peng,S
AU  - Liang,Z
AU  - Luo,C
AU  - Yang,Y
AU  - Jiang,H
AU  - Huang,M
AU  - Chai,W
AU  - Ding,J
AU  - Geng,M
DO  - 10.1371/journal.pone.0037427
PY  - 2012///
SN  - 1932-6203
TI  - Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling
T2  - PLoS ONE
UR  - http://dx.doi.org/10.1371/journal.pone.0037427
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000305345300039&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/58360
VL  - 7
ER  -
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