The HSP90-SGT1 chaperone complex for NLR immune sensors

Abstract

The nucleotide-binding domain and leucine-rich repeat-containing (NLR) proteins function as immune sensors in both plants and animals. NLR proteins recognize, directly or indirectly, pathogen-derived molecules and trigger immune responses. To function as a sensor, NLR proteins must be correctly folded and maintained in a recognition-competent state in the appropriate cellular location. Upon pathogen recognition, conformational changes and/or translocation of the sensors would activate the downstream immunity signaling pathways. Misfolded or used sensors are a threat to the cell and must be immediately inactivated and discarded to avoid inappropriate activation of downstream pathways. Such maintenance of NLR-type sensors requires the SGT1-HSP90 pair, a chaperone complex that is structurally and functionally conserved in eukaryotes. Deciphering how the chaperone machinery works would facilitate an understanding of the mechanisms of pathogen recognition and signal transduction by NLR proteins in both plants and animals.