Hop/Sti1 and Hsp90 Are Involved in Maturation and Transport of a PAMP Receptor in Rice Innate Immunity

• Chen Letian

  NAIST, Japan

• Hamada Satoshi

  NAIST, Japan

• Fujiwara Masayuki

  NAIST, Japan

• Zhu Tingheng

  NAIST, Japan

• Thao Nguyen Phuong

  NAIST, Japan

• Wong Hann Ling

  NAIST, Japan

• Krishna Priti

  Univ. of Western Ontario, Canada

• Ueda Takashi

  Univ. of Tokyo, Japan

• Kaku Hanae

  Fac. of Agr., Meiji Univ. Japan

• Shibuya Naoto

  Fac. of Agr., Meiji Univ. Japan

• Kawasaki Tsutomu

  NAIST, Japan

• Shimamoto Ko

  NAIST, Japan

Abstract

Plants have evolved innate immunity systems to fight pathogen infection. Pathogen-associated molecular patterns (PAMPs) receptors are receptor-like kinases (RLKs) in plants. However, the maturation and transport of PAMP receptors are not well understood. Here, we characterize the Hsp90 co-chaperone Hop/Sti1, a novel OsRac1 interactor. Hop/Sti1 and cytoplasmic Hsp90 bind the rice chitin receptor OsCERK1 in the endoplasmic reticulum (ER). The OsCERK1 complex is then transported to the plasma membrane (PM) via the Sar1-dependent trafficking system. Impairment of Hop/Sti1 and Hsp90 function reduces the efficiency of OsCERK1 transport to the PM. Hop/Sti1a acts in chitin-triggered defense and rice blast resistance. Our results suggest that Hop/Sti1 and Hsp90 may function to link PAMP receptors and Rac/Rop GTPases. The Hop/Sti1a-Hsp90 chaperone complex appears to have a highly conserved role in the maturation and transport of receptors and ion channels in plants and animals.

Journal

• Plant and Cell Physiology Supplement

  Plant and Cell Physiology Supplement 2010 (0), 0183-0183, 2010

  The Japanese Society of Plant Physiologists

Details

• CRID: 1390001205630996352
• NII Article ID: 130006991976
• DOI: 10.14841/jspp.2010.0.0183.0
• Data Source:
  • JaLC
  • CiNii Articles
• Abstract License Flag: Disallowed