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International Immunology, Vol. 12, No. 4, 573-580, April 2000
© 2000 Japanese Society for Immunology

A BASH/SLP-76-related adaptor protein MIST/Clnk involved in IgE receptor-mediated mast cell degranulation

Ryo Goitsuka1,2, Hideki Kanazashi1, Hiroki Sasanuma1, Yu-ichi Fujimura1, Yuri Hidaka1, Akiko Tatsuno1, Chisei Ra3, Katsuhiko Hayashi1 and Daisuke Kitamura1

1 Division of Molecular Biology, Research Institute for Biological Sciences, Science University of Tokyo, 2669 Yamazaki, Noda, Chiba 278, Japan
2 Inheritance and Variation Group, PRESTO, Japan Science and Technology Corp., 2669 Yamazaki, Noda, Chiba 278, Japan
3 Division of Molecular Biology, Allergy Research Center, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

Correspondence to: R. Goitsuka, Division of Molecular Biology, Research Institute for Biological Sciences, Science University of Tokyo, 2669 Yamazaki, Noda, Chiba 278, Japan

Cross-linking of the high-affinity IgE receptor (Fc{epsilon}RI) on mast cells by IgE–antigen complex triggers signal transduction cascades leading to the release of inflammatory mediators and production of cytokines, which are critical for the development of allergic reactions. We have identified a novel member of the BASH/SLP-76 immunoreceptor-coupled adaptor family expressed in mast cells, termed MIST (for mast cell immunoreceptor signal transducer), which has later been found to be identical to a recently reported cytokine-dependent hemopoietic cell linker, Clnk. Upon Fc{epsilon}RI cross-linking, MIST/Clnk is tyrosine phosphorylated and associates with signaling proteins, phospholipase C{gamma}, Vav, Grb2 and linker for activation of T cells (LAT). Overexpression of a mutant form of MIST/Clnk inhibited Fc{epsilon}RI-mediated degranulation, increase in intracellular Ca2+, NF-AT activation and phosphorylation of LAT. As a crucial signaling component for Fc{epsilon}RI-induced mast cell degranulation, MIST/Clnk might serve as a target for anti-allergic therapy.

Keywords: Fc{varepsilon}RI, RBL, signal transduction

Transmitting editor: K. Okumura


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