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IL‐2‐induced gene expression of protein‐tyrosine phosphatase LC‐PTP requires acidic and serine‐rich regions within IL‐2 receptor β chain
Author(s) -
Adachi Masaaki,
Torigoe Toshihiko,
Sekiya Masuo,
Minami Yasuhiro,
Taniguchi Tadatsugu,
Hinoda Yuji,
Yachi Akira,
Reed John C.,
Imai Kohzoh
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00952-6
Subject(s) - protein tyrosine phosphatase , microbiology and biotechnology , serine , tyrosine kinase , chemistry , kinase , messenger rna , gene expression , receptor tyrosine kinase , phosphatase , signal transduction , biology , gene , phosphorylation , biochemistry
A protein‐tyrosine phosphatase LC‐PTP is preferentially expressed in hematopoietic cells and is an early response gene in lymphokine stimulated cells. Here, we found the LC‐PTP mRNA induction by IL‐2 was markedly inhibited by several tyrosine kinase inhibitors. The induction required both the acidic and serine‐rich regions of the IL‐2 receptor β chain (IL‐2Rβ) in mouse IL‐3‐dependent pro‐B BAF‐B03 transfectants. This is strikingly different from the induction of c‐ myc gene expression, which requires the serine‐rich region alone. In addition, overexpression of activated‐Lck or ‐Raf kinases resulted in augmented LC‐PTP mRNA expression in myeloid cell line 32D transfectants. Considering the previous findings that the acidic region of the IL‐2Rβ is responsible for association with Lck and activation of Raf kinase, IL‐2‐induced expression of LC‐PTP mRNA may be primarily transduced through a Lck‐Raf mediated signaling pathway.