Rice immune regulator, OsPti1a, is specifically phosphorylated at the plasma membrane.
OsPti1a (Pto-interacting protein 1a) has important roles in the regulation of immune responses in rice. Phosphorylation of a conserved threonine in OsPti1a is necessary to activate defense responses; however, the regulatory mechanism of OsPti1a-mediated immune responses is still obscure. Recently, we revealed that OsPti1a forms protein complex(es) at the plasma membrane and this localization is required for its function. Here, we show that membrane-localized OsPti1a was selectively phosphorylated. Additionally, phosphorylation was not required for the localization of OsPti1a at the membrane. These results suggest that OsPti1a protein is selectively regulated by its phosphorylation after OsPti1a localizes to the plasma membrane.
a Plant Proteomics Research Unit; RIKEN Center for Sustainable Resource Science ; Suehiro-cho; Tsurumi-ku; Yokohama , Kanagawa , Japan.
Hidenori
H
Matsui
Akira
A
Takahashi
Hirohiko
H
Hirochika
D002462:Cell Membrane / Q000378:metabolism*; D060467:Disease Resistance; D012275:Oryza / Q000378:metabolism*; D010766:Phosphorylation; D010935:Plant Diseases; D010940:Plant Proteins / Q000378:metabolism*; D021381:Protein Transport; D013912:Threonine / Q000378:metabolism
D010940:Plant Proteins; D013912:Threonine
HR, hypersensitive response; Pti1; Pti1, Pto-interacting protein 1.; phosphorylation; plant immunity; plasma membrane; rice