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Updated: Apr 16, 2026

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
Published on: June 25, 2020
Rice immune regulator, OsPti1a, is specifically phosphorylated at the plasma membrane
Hidenori Matsui1, Akira Takahashi, Hirohiko Hirochika
1a Plant Proteomics Research Unit; RIKEN Center for Sustainable Resource Science ; Suehiro-cho; Tsurumi-ku; Yokohama , Kanagawa , Japan.
Abstract:
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.
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