Fyn binds to and phosphorylates T cell immunoglobulin and mucin domain-1 (Tim-1)

Miranda L. Curtiss, Bruce S. Hostager, Elizabeth Stepniak, Melody Singh, Natalie Manhica, Judit Knisz, Geri Traver, Paul D. Rennert, John D. Colgan, Paul B. Rothman

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1424-1431
Number of pages8
JournalMolecular Immunology
Issue number12-13
StatePublished - Jul 2011
Externally publishedYes


  • B cell
  • Fyn
  • Havcr-1
  • Signaling
  • Tim-1

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology


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