Dissociation of hp-IRAK1:TRAF6 or IRAK2:TRAF6-oligomer from the activated TLR5 or 10:oligo-Myd88:p-IRAK4 complex

Hyperphosphorylated IRAK1 and TRAF6 are thought to dissociate from the activated receptor. (Gottipati et al. 2007) but the IRAK1:TRAF6 complex may remain associated with the membrane (Dong et al. 2006).<p> Phosphorylated IRAK2, like its paralog IRAK1, possibly dissociates from the activated receptor as shown here, although mechanism of IRAK2 activation by IRAK4 followed by TRAF6 binding remains to be deciphered.

高磷酸化的 IRAK1 和 TRAF6 据推测可能从激活的受体上解离（Gottipati 等人，2007年），然而，IRAK1:TRAF6 复合物可能仍然与膜保持结合（Dong 等人，2006年）。磷酸化的 IRAK2，如同其同源基因 IRAK1，可能如本例所示从激活的受体上解离，尽管 IRAK2 由 IRAK4 激活并随后与 TRAF6 结合的机制尚待阐明。