| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2045964 | Current Opinion in Plant Biology | 2011 | 7 Pages |
Plant disease resistance proteins commonly belong to the nucleotide binding-leucine rich repeat (NB-LRR) protein family. These specialized immune proteins mediate recognition of diverse pathogen-derived effector proteins and initiate potent defense responses. NB-LRRs exhibit a multidomain architecture and each domain appears to have discrete functions depending on the stage of NB-LRR signaling. Novel proteins that were found to interact with the core HSP90 chaperone complex regulate accumulation and activation of NB-LRR immune receptors. Recent studies have also advanced our understanding of how accessory proteins contribute to NB-LRR activation. The dynamic nature of NB-LRR localization to different subcellular compartments before and after activation suggests that NB-LRRs may activate immune responses in multiple parts of the cell. In this review we highlight recent advances in understanding NB-LRR function.
► NB-LRRs are specialized immune proteins that recognize specific pathogen proteins. ► NB-LRRs require a conserved chaperone complex for proper function. ► New regulators of NB-LRR accumulation and activation have been identified. ► Recent evidence suggests that NB-LRRs activate immunity in the cytoplasm and nucleus.
