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 ...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/β-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.展开更多
基金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)
文摘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/β-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.
