| First Author | Hahn JS | Year | 2005 |
| Journal | FEBS Lett | Volume | 579 |
| Issue | 20 | Pages | 4513-9 |
| PubMed ID | 16083881 | Mgi Jnum | J:200305 |
| Mgi Id | MGI:5508264 | Doi | 10.1016/j.febslet.2005.07.024 |
| Citation | Hahn JS (2005) Regulation of Nod1 by Hsp90 chaperone complex. FEBS Lett 579(20):4513-9 |
| abstractText | Nod1 and Nod2 proteins play important roles in mammalian innate immune responses as intracellular sensors for bacterial peptidoglycan. Nod1 and Nod2 share structural homology with many R proteins involved in plant disease resistance. It has been demonstrated that plant Hsp90 and its co-chaperone RAR1 are implicated in R-mediated disease resistance. Here the Chp-1 gene encoding a mammalian homologue of plant RAR1 was identified as a new target for transcriptional activation by heat shock factor 1 (HSF1), a stress-responsive HSF isoform. In addition, Nod1 is demonstrated to be a client protein of the Hsp90 chaperone complex containing the Chp-1. Chp-1 interacts with the tetratricopeptide repeat (TPR) domain of protein phosphatase 5 (PP5) and the ATPase domain of Hsp90 via two distinct zinc-binding cysteine and histidine rich domains (CHORDs). These findings suggest a common regulatory mechanism involving the Hsp90 chaperone complex in R-mediated disease resistance in plants and Nod1-mediated innate immune response in mammals. |
