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TIM‐1 signaling in T cell activation
Author(s) -
Lin Jean YeanJin,
Kane Lawrence P.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.663.26
Subject(s) - phosphorylation , tyrosine phosphorylation , microbiology and biotechnology , signal transduction , t cell , cell signaling , tyrosine , proto oncogene tyrosine protein kinase src , chemistry , protein tyrosine phosphatase , immune system , biology , biochemistry , immunology
T cell immunoglobulin and mucin 1 (TIM‐1) is capable of acting as a co‐stimulatory molecule to enhance T cell activation and to modulate CD4+ T cell responses. Currently, relatively little is known about the signal transduction pathways downstream of TIM‐1 that are responsible for controlling these immune responses. Previous work from this laboratory has demonstrated that src‐kinase dependent tyrosine phosphorylation of the cytoplasmic tail of TIM‐1 is important in transmitting the TIM‐1 response in the T cell. The purpose of this study is to explore additional tyrosine phosphorylated proteins that may be downstream of TIM‐1 signaling. Whole cell lysates from TIM‐1 stimulated D10 cells were probed for tyrosine phosphorylation. This work has suggested a previously unrecognized phosphorylated substrate that can be induced by agonistic anti‐TIM‐1 antibodies. We are currently working to identify this protein as well as to better define the conditions under which it is phosphorylated. Supported by NIAID and NCI.