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Wild soybean SNARE proteins BET1s mediate the subcellular localization of the cytoplasmic receptor‐like kinases CRCK1s to modulate salt stress responses
Author(s) -
Sun Xiaoli,
Cai Xiaoxi,
Yin Kuide,
Gu Liwei,
Shen Yang,
Hu Bingshuang,
Wang Yan,
Chen Yue,
Zhu Yanming,
Jia Bowei,
Sun Mingzhe
Publication year - 2021
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.15072
Subject(s) - subcellular localization , bimolecular fluorescence complementation , arabidopsis , microbiology and biotechnology , kinase , biology , transmembrane domain , transmembrane protein , cytoplasm , biochemistry , glycine , receptor , amino acid , gene , mutant
Summary Plants have evolved numerous receptor‐like kinases (RLKs) that modulate environmental stress responses. However, little is known regarding soybean ( Glycine max ) RLKs. We have previously identified that Glycine soja Ca 2+ /CAM‐binding RLK (GsCBRLK) is involved in salt tolerance. Here, we report that soluble NSF attachment protein receptor proteins BET1s mediate subcellular localization of calmodulin‐binding receptor‐like cytoplasmic kinases CRCK1s to modulate salt stress responses. Direct interaction between GsCBRLK and GsBET11a was initially identified via yeast two‐hybrid and bimolecular fluorescence complementation assays. Further analysis demonstrated conserved interaction between BET1s and CRCK1s. GsCBRLK interacted with all BET1 proteins in wild soybean ( Glycine soja ) and Arabidopsis, and GsBET11a strongly associated with GsCRCK1a–1d, but slightly with AtCRCK1. In addition, GsBET11a interacted with GsCBRLK via its C‐terminal transmembrane domain (TMD), where the entire TMD, not the sequence, was critical for the interaction. Moreover, the N‐terminal variable domain (VD) of GsCBRLK was responsible for interacting with GsBET11a, and the intensity of interaction between GsCBRLK/AtCRCK1 and GsBET11a was dependent on VD. Furthermore, GsBET11a was able to mediate the GsCBRLK subcellular localization via direct interaction with VD. Additionally, knockout of AtBET11 or AtBET12 individually did not alter GsCBRLK localization, while GsBET11a expression caused partial internalization of GsCBRLK from the plasma membrane (PM). We further suggest the necessity of GsCBRLK VD for its PM localization via N‐terminal truncation assays. Finally, GsBET11a was shown to confer enhanced salt stress tolerance when overexpressed in Arabidopsis and soybean. These results revealed the conserved and direct interaction between BET1s and CRCK1s, and suggested their involvement in salt stress responses.