Functions of RPM1-interacting protein 4 in plant immunity.

Planta

State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Taian, 271018, Shandong, People's Republic of China.

Published: January 2021

AI Article Synopsis

  • The article reviews recent research on RPM1-interacting protein 4 (RIN4), highlighting its crucial role in plant immunity through posttranslational modifications and regulation of related proteins.
  • RIN4 is involved in both pathogen-triggered immunity (PTI) and effector-triggered immunity (ETI), interacting with key proteins like PM H-ATPase and EXO70, and is modified by pathogenic effector proteins.
  • The review focuses on the structural features of RIN4, including its conserved domains and cysteine residues essential for function, while also discussing advancements in identifying RIN4-associated NLR proteins across different plant species.

Article Abstract

We reviewed recent advances related to RIN4, including its involvement in the immune process through posttranslational modifications, PM H-ATPase activity regulation, interaction with EXO70 and identification of RIN4-associated NLR proteins. RPM1-interacting protein 4 (RIN4) is a conserved plant immunity regulator that has been extensively studied and can be modified by pathogenic effector proteins. RIN4 plays an important role in both PTI and ETI. In this article, we review the functions of the two conserved NOI domains of RIN4, the C-terminal cysteine residues required for membrane localization and the sites targeted and modified by effector proteins during plant immunity. In addition, we discuss the effect of RIN4 on the stomatal virulence of pathogens via the regulation of PM H-ATPase activity, which is involved in the immune process through interactions with the exocyst subunit EXO70, and progress in the identification of RIN4-related R proteins in multiple species. This review provides new insights enhancing the current understanding of the immune function of RIN4.

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Source
http://dx.doi.org/10.1007/s00425-020-03527-7DOI Listing

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