Imperial College London
Portrait Picture

Dr Woscholski

Faculty of Natural Sciences, Department of Chemistry

Reader in Chemical Biology
 
 
 
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Contact

 

+44 (0)20 7594 5305r.woscholski

 
 
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Location

 

301LMolecular Sciences Research HubWhite City Campus

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Summary

 

Publications

Citation

BibTex format

@article{Verrastro:2016:10.1016/j.freeradbiomed.2015.11.004,
author = {Verrastro, I and Tveen-Jensen, K and Woscholski, R and Spickett, CM and Pitt, AR},
doi = {10.1016/j.freeradbiomed.2015.11.004},
journal = {Free Radical Biology and Medicine},
pages = {24--34},
title = {Reversible oxidation of phosphatase and tensin homolog (PTEN) alters its interactions with signaling and regulatory proteins},
url = {http://dx.doi.org/10.1016/j.freeradbiomed.2015.11.004},
volume = {90},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Phosphatase and tensin homolog (PTEN) is involved in a number of different cellular processes including metabolism, apoptosis, cell proliferation and survival. It is a redox-sensitive dual-specificity protein phosphatase that acts as a tumor suppressor by negatively regulating the PI3K/Akt pathway. While direct evidence of redox regulation of PTEN downstream signaling has been reported, the effect of PTEN redox status on its protein–protein interactions is poorly understood. PTEN-GST in its reduced and a DTT-reversible H2O2-oxidized form was immobilized on a glutathione-sepharose support and incubated with cell lysate to capture interacting proteins. Captured proteins were analyzed by LC–MSMS and comparatively quantified using label-free methods. 97 Potential protein interactors were identified, including a significant number that are novel. The abundance of fourteen interactors was found to vary significantly with the redox status of PTEN. Altered binding to PTEN was confirmed by affinity pull-down and Western blotting for Prdx1, Trx, and Anxa2, while DDB1 was validated as a novel interactor with unaltered binding. These results suggest that the redox status of PTEN causes a functional variation in the PTEN interactome. The resin capture method developed had distinct advantages in that the redox status of PTEN could be directly controlled and measured.
AU  - Verrastro,I
AU  - Tveen-Jensen,K
AU  - Woscholski,R
AU  - Spickett,CM
AU  - Pitt,AR
DO  - 10.1016/j.freeradbiomed.2015.11.004
EP  - 34
PY  - 2016///
SN  - 0891-5849
SP  - 24
TI  - Reversible oxidation of phosphatase and tensin homolog (PTEN) alters its interactions with signaling and regulatory proteins
T2  - Free Radical Biology and Medicine
UR  - http://dx.doi.org/10.1016/j.freeradbiomed.2015.11.004
UR  - http://hdl.handle.net/10044/1/32806
VL  - 90
ER  -
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