Fyn binds to and phosphorylates T cell immunoglobulin and mucin domain-1 (Tim-1)
2011
Curtiss, Miranda L. | Hostager, Bruce S. | Stepniak, Elizabeth | Singh, Melody | Manhica, Natalie | Knisz, Judit | Traver, Geri | Rennert, Paul D. | Colgan, John D. | Rothman, Paul B.
The gene encoding T cell immunoglobulin and mucin domain-1 (Tim-1) is linked to atopy and asthma susceptibility in mice and humans. Tim-1 is a transmembrane protein expressed on activated lymphocytes and appears to have a role as a co-stimulatory receptor in T cells. The protein has not been shown to have enzymatic activity but contains a site within its cytoplasmic tail predicted to be a target for tyrosine kinases. Here, we show that Tim-1 can associate with the kinase Fyn, a member of the Src family of tyrosine kinases. This association does not require Fyn's kinase activity and is independent of the phosphorylation of a conserved tyrosine present within the cytoplasmic tail of Tim-1. Fyn is necessary for phosphorylation of this tyrosine in Tim-1 and the phosphorylation of Tim-1 varies with the levels of Fyn present in cells. These data suggest a role for Fyn in the signaling downstream of Tim-1.
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