P-341 - A karyopherin mediates nuclear shuttling of ADR1 helper NLRs to regulate plant immunity

 Nucleotide-binding domain and leucine-rich repeat (NLR) proteins are important intracellular immune receptors that activate robust plant immune responses upon recognizing pathogen-secreted effector proteins. NLRs-mediated cell death and disease resistance signaling are closely related to their subcellular localization. To date, a large number of regulatory factors have been identified that affect the nucleocytoplasmic transport and subcellular localization of sensor NLRs. It is still unclear whether helper NLRs display nuclear translocation and the impact of their different subcellular distributions on their immune function is still obscure. Here we show that ADR1 class helper NLRs relocate from the plasma membrane into nucleus following ETI activation. We identified a karyopherin-β protein transportin1 as an interacting protein of ADR1-L1 by immunoprecipitation coupled to mass spectrometry (IP-MS). We found that transportin1 can directly interact with ADR1 family proteins and transport ADR1s into the nucleus. Moreover, overexpression of transportin1 is able to suppress the ADR1s-mediated autoimmunity and inhibit ADR1s-mediated cell death. Thus, our results provide new insights for understanding the relationships between the subcellular localization of helper NLRs and their immune functions.