These authors contributed equally to this work
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Proteome identification of binding-partners interacting with cell polarity protein Par3 in Jurkat cells
Article first published online: 12 AUG 2008
DOI: 10.1111/j.1745-7270.2008.00452.x
© 2008 Institute of Biochemistry and Cell Biology, SIBS, CAS
Additional Information
How to Cite
Zhou, Y., Fang, L., Du, D., Zhou, W., Feng, X., Chen, J., Zhang, Z. and Chen, Z. (2008), Proteome identification of binding-partners interacting with cell polarity protein Par3 in Jurkat cells. Acta Biochimica et Biophysica Sinica, 40: 729–739. doi: 10.1111/j.1745-7270.2008.00452.x
Publication History
- Issue published online: 12 AUG 2008
- Article first published online: 12 AUG 2008
- Received: April 3, 2008 Accepted: May 11, 2008
- Abstract
- References
- Cited By
Keywords:
- cell polarity;
- Par3;
- proteomics;
- importin-α4;
- PA28β;
- PA28γ
The evolutionarily conserved cell polarity protein Par3, a scaffold-like PDZreontaining protein, plays a critical role in the establishment and maintenance of epithelial cell polarity. Although the role of Par3 in establishing cell polarity in epithelial cells has been intensively explored, the function of Par3 in hematopoietic cells remains elusive. To address this issue, we generated GST-fusion proteins of Par3 PDZ domains. By combiningthe GST-pull-down approach with liquid chromatography-tandem mass spectrometry, we identified 10 potential novel binding proteins of PDZ domains of Par3 in Jurkat cells (a T-cell line). The interaction of Par3 with three proteins—nuclear transport protein importin-α4 and proteasome activators PA28β and PA28γ—was confirmed using in vitro binding assay, co-immunoprecipitation assay and immunofluorescence microscopy. Our results have the potential to uncover novel functions of the cell polarity protein Par3 in blood cells.