CRCU

Chemical Research in Chinese Universities ›› 2011, Vol. 27 ›› Issue (3): 474-477.

• Articles • Previous Articles     Next Articles

Expression and Characterization of the Intracellular Part of Receptor Protein Tyrosine Phosphatase PTPRU

WANG Shao-feng1,2, HAN Jia-yu2, FU Xue-qi1* and ZHAO Zhi-zhuang Joe1,2*   

  1. 1. Edmond H. Fischer Signal Transduction Laboratory, College of Life Sciences, Jilin University, Changchun 130012, P. R. China;
    2. Department of Pathology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma?73104, USA
  • Received:2010-03-08 Revised:2010-04-30 Online:2011-05-25 Published:2011-04-29
  • Contact: FU Xue-qi and ZHAO Zhi-zhuang Joe E-mail:fxq@jlu.edu.cn; joe-zhao@ouhsc.edu
  • Supported by:

    Supported by the Grant from the Plan for Development of Science & Technology in Jilin Province, China(No.20090920),  the Boyou Fund from China Soong Ching Ling Foundation and the Grant from the National Institutes of Health, USA (No.HL76309).

PDF (PC)

Cited

1

Abstract: PTPRU is an MAM domain-containing receptor-like protein tyrosine phosphatase. Previous studies have demonstrated an important role of the enzyme in the maintenance of epithelial integrity and in the regulation of the Wnt/?-catenin signaling pathway. To better understand the function of PTPRU, we cloned and expressed the intracellular portion of PTPRU as a GST fusion protein in E. coli cells. We purified the protein to homogeneity and used it to immunize mice for antibody production. The resultant antibody specifically recognized PTPRU over-expressed in the cell line. Western blot analyses demonstrated the partition of truncated forms of PTPRU containing the cadherin-like domain in the Triton X-100-insoluble fraction, and immunofluorescent cell staining revealed the localization of these proteins in punctate intracellular structures. Our data suggest that the cadherin-like domain of PTPRU has a major role in determining its intracellular localization.

Key words: Tyrosine phosphatase, Cadherin, Catenin, Microdomain