Skip to main content
. 2007 Dec 26;28(5):1841–1850. doi: 10.1128/MCB.01468-07

FIG. 6.

FIG. 6.

Nucleotide binding by Monarch-1 is required for the suppression of IRAK-1 hyperphosphorylation. (A) THP-WT or THP-mutA/B cells were stimulated for the indicated times with Pam3Cys4. Endogenous IRAK-1 was immunoprecipitated (IP), and Western blots (IB) were probed with anti-HA to detect Monarch-1. Control samples were immunoprecipitated with an isotype-matched antibody. Control Western blottings were performed on cellular lysates to monitor the levels of Monarch-1 and IRAK-1. (B) THP-EV, THP-WT, and THP-mutA/B cells were stimulated with Pam3Cys4 for the indicated times. Lysates were separated by SDS-PAGE, and Western blots were probed with anti-IRAK-1 antibodies. Control Western blottings were performed and probed with anti-HA to monitor Monarch-1 expression. These results are representative of at least five separate experiments.