Dec, 2014
Effects of protein tyrosine phosphatase-PEST are reversed by Akt in T cells
CELLULAR SIGNALLING
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- Volume
- 26
- Number
- 12
- First page
- 2721
- Last page
- 2729
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1016/j.cellsig.2014.08.014
- Publisher
- ELSEVIER SCIENCE INC
T cell activation is regulated by a balance between phosphorylation and dephosphorylation that is under the control of kinases and phosphatases. Here, we examined the role of a non-receptor-type protein tyrosine phosphatase, PTP-PEST, using retrovirus-mediated gene transduction into murine T cells. Based on observations of vector markers (GFP or Thy1.1), exogenous PTP-PEST-positive CD4(+) T cells appeared within 2 days after gene transduction; the percentage of PIP-PEST-positive cells tended to decrease during a resting period in the presence of IL-2 over the next 2 days. These vector markers also showed much lower expression intensities, compared with control cells, suggesting a correlation between the percent reduction and the low marker expression intensity. A catalytically inactive PIP-PEST mutant also showed the same tendency, and stepwise deletion mutants gradually lost their ability to induce the above phenomenon. On the other hand, these PIP-PEST-transduced cells did not have an apoptotic phenotype. No difference in the total cell numbers was found in the wells of a culture plate containing VEC- and PIP-PEST-transduced T cells. Moreover, serine/threonine kinase Akt, but not the anti-apoptotic molecules Bc1-2 and Bcl-XL, reversed the phenotype induced by PTP-PEST. We discuss the novel mechanism by which Ala interferes with PIP-PEST. (C) 2014 Elsevier Inc. All rights reserved.
- Link information
- ID information
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- DOI : 10.1016/j.cellsig.2014.08.014
- ISSN : 0898-6568
- eISSN : 1873-3913
- Pubmed ID : 25152368
- Web of Science ID : WOS:000345107700015