Literature DB >> 20227662

The Hop/Sti1-Hsp90 chaperone complex facilitates the maturation and transport of a PAMP receptor in rice innate immunity.

Letian Chen1, Satoshi Hamada, Masayuki Fujiwara, Tingheng Zhu, Nguyen Phuong Thao, Hann Ling Wong, Priti Krishna, Takashi Ueda, Hanae Kaku, Naoto Shibuya, Tsutomu Kawasaki, Ko Shimamoto.   

Abstract

Recognition of pathogen-associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs) represents a critical first step of innate defense in plants and animals. However, maturation and transport of PRRs are not well understood. We find that the rice chitin receptor OsCERK1 interacts with Hsp90 and its cochaperone Hop/Sti1 in the endoplasmic reticulum (ER). Hop/Sti1 and Hsp90 are required for efficient transport of OsCERK1 from the ER to the plasma membrane (PM) via a pathway dependent on Sar1, a small GTPase which regulates ER-to-Golgi trafficking. Further, Hop/Sti1 and Hsp90 are present at the PM in a complex (designated the "defensome") with OsRac1, a plant-specific Rho-type GTPase. Finally, Hop/Sti1 was required for chitin-triggered immunity and resistance to rice blast fungus. Our results suggest that the Hop/Sti1-Hsp90 chaperone complex plays an important and likely conserved role in the maturation and transport of PRRs and may function to link PRRs and Rac/Rop GTPases. Copyright 2010 Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 20227662     DOI: 10.1016/j.chom.2010.02.008

Source DB:  PubMed          Journal:  Cell Host Microbe        ISSN: 1931-3128            Impact factor:   21.023


  65 in total

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9.  Arabidopsis Endoplasmic Reticulum-Localized UBAC2 Proteins Interact with PAMP-INDUCED COILED-COIL to Regulate Pathogen-Induced Callose Deposition and Plant Immunity.

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