Abstract:
:Properly regulated mitogen-activated protein (MAP) kinase activity is critical for normal thymocyte development. MAP kinases are activated by phosphorylation of tyrosine and threonine, and dual specificity phosphatases (DUSPs) can inactivate MAP kinases by dephosphorylating both tyrosine and threonine. However, a role for DUSPs in thymocyte development has not been described. In this study, we have defined the subset of DUSP genes expressed in the murine thymus, and how their expression varies in different thymocyte subsets. Of the murine DUSP genes screened that could potentially dephosphorylate MAP kinases, we found 10 transcribed in the thymus. Seven of these 10 thymic DUSPs are true MAP kinase phosphatases based on the presence of a MAP kinase binding domain and demonstrated phosphatase activity against MAP kinases. Six of the seven thymic MAP kinase phosphatases have been shown to dephosphorylate extracellular regulated kinase (ERK). Quantitative PCR analysis of thymocyte populations isolated from different developmental stages revealed significant changes in DUSP expression as thymocytes progressed through development. Specifically, DUSPs 1, 4, and 5 significantly increase in expression as cells go from small, resting CD4/CD8 double positive cells to the CD4 single positive stage. Additionally, in vitro experiments showed that DUSPs could respond to TCR signaling, as anti-CD3 stimulation of thymocytes transiently increased transcription of six of the 10 thymic DUSP genes within 30 min. Notably, the ERK-specific phosphatase DUSP5 was upregulated 43-fold within 30 min, and returned to baseline within 24 h. Overall, we have identified a subset of DUSPs that could potentially regulate ERK activation in response to TCR signals in thymocytes.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Tanzola MB,Kersh GJdoi
10.1016/j.molimm.2005.03.006subject
Has Abstractpub_date
2006-02-01 00:00:00pages
754-62issue
6eissn
0161-5890issn
1872-9142pii
S0161-5890(05)00068-4journal_volume
43pub_type
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