Collaboration work with Scripps and Hebrew University was introduced in JACI.

Phosphorylation triggers the structural and functional switch of a housekeeping protein for mast cells 

Cross-linking of IgE receptors on the surfaces of mast cells results in the synthesis of a number of mediators that is regulated by the transcription factor microphthalmia-associated transcription factor (MITF). Activation of MITF requires the production of the antigen-IgE–induced second messenger diadenosine tetraphosphate (Ap4A). Prior studies have demonstrated a role for lysyl-tRNA synthetase (LysRS), an aminoacyl tRNA synthetase that catalyzes the assignment of lysine to a tRNA as part of the fundamental machinery in protein translation in MITF activation, but the mechanism for regulation of these 2 distinct functions for LysRS is unknown. Studies performed by Ofir-Birin et al (Mol Cell 2013;49:30-42) delineate a cascade of events triggered by phosphorylation of LysRS after activation of the IgE receptor that leads to a strong conformational change, followed by translocation of LysRS from the cytoplasm to the nucleus, where it binds to MITF and generates Ap4A to activate transcription of MITF target genes (see video available at Their findings establish a unique switch mechanism using housekeeping proteins for prompt induction of inflammatory mediators by activated mast cells.

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We asked authors Ehud Razin from the Institute for Medical Research Israel-Canada/Hebrew University–Hadassah Medical School and Min Guo from the Scripps Research Institute to comment on the significance of these results: “This will allow [us] to obtain a unique insight regarding the physiological significance of the second messenger, Ap4A, in mast cell function and in allergic related diseases.”

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   Professor Ehud Razin and Min Guo, PhD

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