Conceptual diagram of the present study (IMAGE)
Caption
LECT2 suppresses the recruitment of SHP2/c-Cbl to MET, which is known to promote proteasome degradation of RIG-I, by selectively suppressing the phosphorylation of the 1349th tyrosine of the HGF receptor MET. LECT2 promotes the recruitment of the second protein tyrosine phosphatase, PTP4A1, to MET and PTP4A1 dephosphorylates SHP2 under ligand-free conditions. Thus, PTP4A1 and SHP2 have antagonistic effects on MET, and the antagonism of these phosphatases that bind to MET is essential for maintaining a normal homeostatic balance. When cells are infected with a virus, LECT2 functions as the primary ligand for MET, shifting the balance to the involvement of PTP4A1 and resulting in enhanced RIG-I-dependent innate immune responses. On the other hand, in tissue repair and cancer, HGF is the main ligand for MET, suppressing the innate immune responses and enhancing the growth signal. The research team has revealed the existence of crosstalk between the innate immune responses and MET-dependent proliferation in the liver.
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Kanazawa University
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