TY - JOUR
T1 - Plasma membrane localization is essential for oryza sativa pto-interacting protein 1a-mediated negative regulation of immune signaling in rice
AU - Matsui, Hidenori
AU - Matsui, Hidenori
AU - Fujiwara, Masayuki
AU - Hamada, Satoshi
AU - Shimamoto, K.
AU - Nomura, Yuko
AU - Nakagami, Hirofumi
AU - Takahashi, Akira
AU - Hirochika, Hirohiko
N1 - Publisher Copyright:
© 2014. American Society of Plant Biologists. All rights reserved.
PY - 2014/9/1
Y1 - 2014/9/1
N2 - Oryza sativa Pto-interacting protein 1a (OsPti1a), an ortholog of tomato (Solanum lycopersicum) SlPti1, functions as a negative regulator of innate immunity in rice (Oryza sativa). In ospti1a mutants, the activation of immune responses, including hypersensitive response-like cell death, is caused by loss of the OsPti1a protein; however, it is as yet unclear how OsPti1a suppresses immune responses. Here, we report that OsPti1a localizes to detergent-resistant membrane fractions of the plasma membrane through lipid modification of the protein’s amino terminus, which is highly conserved among Pti1 orthologs in several plant species. Importantly, mislocalization of OsPti1a after deletion of its amino terminus reduced its ability to complement the mutant phenotypes, including hypersensitive response-like cell death. Furthermore, complex formation of OsPti1a depends on its amino terminus-mediated membrane localization. Liquid chromatography-tandem mass spectrometry analysis of OsPti1a complexinteracting proteins identified several defense-related proteins. Collectively, these findings indicate that appropriate complex formation by OsPti1a at the plasma membrane is required for the negative regulation of plant immune responses in rice.
AB - Oryza sativa Pto-interacting protein 1a (OsPti1a), an ortholog of tomato (Solanum lycopersicum) SlPti1, functions as a negative regulator of innate immunity in rice (Oryza sativa). In ospti1a mutants, the activation of immune responses, including hypersensitive response-like cell death, is caused by loss of the OsPti1a protein; however, it is as yet unclear how OsPti1a suppresses immune responses. Here, we report that OsPti1a localizes to detergent-resistant membrane fractions of the plasma membrane through lipid modification of the protein’s amino terminus, which is highly conserved among Pti1 orthologs in several plant species. Importantly, mislocalization of OsPti1a after deletion of its amino terminus reduced its ability to complement the mutant phenotypes, including hypersensitive response-like cell death. Furthermore, complex formation of OsPti1a depends on its amino terminus-mediated membrane localization. Liquid chromatography-tandem mass spectrometry analysis of OsPti1a complexinteracting proteins identified several defense-related proteins. Collectively, these findings indicate that appropriate complex formation by OsPti1a at the plasma membrane is required for the negative regulation of plant immune responses in rice.
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U2 - 10.1104/pp.114.243873
DO - 10.1104/pp.114.243873
M3 - Article
C2 - 24958714
AN - SCOPUS:84907059378
SN - 0032-0889
VL - 166
SP - 327
EP - 336
JO - Plant physiology
JF - Plant physiology
IS - 1
ER -