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Phosphorylation of a wheat aquaporin at two sites enhances both plant growth and defense 被引量:4

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摘要 Eukaryotic aquaporins share the characteristic of functional multiplicity in transporting distinct substrates and regulating various processes,but the underlying molecular basis for this is largely unknown.Here,we report that the wheat(Triticum aestivum)aquaporin TaPIP2;10 undergoes phosphorylation to promote photosynthesis and productivity and to confer innate immunity against pathogens and a generalist aphid pest.In response to elevated atmospheric CO_(2)concentrations,TaPIP2;10 is phosphorylated at the serine residue S280 and thereafter transports CO_(2)into wheat cells,resulting in enhanced photosynthesis and increased grain yield.In response to apoplastic H_(2)O_(2) induced by pathogen or insect attacks,TaPIP2;10 is phosphorylated at S121 and this phosphorylated form transports H_(2)O_(2) into the cytoplasm,where H_(2)O_(2)intensifies host defenses,restricting further attacks.Wheat resistance and grain yield could be simultaneously increased by TaPIP2;10 overexpression or by expressing a TaPIP2;10 phosphomimic with aspartic acid substitutions at S121 and S280,thereby improving both crop productivity and immunity.
出处 《Molecular Plant》 SCIE CAS CSCD 2022年第11期1772-1789,共18页 分子植物(英文版)
基金 Natural Science Foundation of China(grants numbers31772247,32072399,and 32170202) Natural Science Foundation of Shandong Province(grants ZR2020MC113,ZR2020MC120,and ZR2020QC126).
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