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Biochem Biophys Res Commun. 2001 Oct 26;288(2):313-20.

Heterogeneity in the phosphorylation of human death receptors by p42(mapk/erk2).

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Program in Cell Biology, National Jewish Medical and Research Center, 1400 Jackson Street, Denver, CO 80206, USA.


Phosphorylation of murine CD120a by p42(mapk/erk2) has been shown to inhibit its ability to initiate apoptosis while preserving signaling events such as NF-kappaB activation. Therefore, we sought to determine if p42(mapk/erk2) was also capable of phosphorylating additional human death receptors within the TNF receptor superfamily. These studies showed that CD120a and DR3 are significantly phosphorylated by p42(mapk/erk2) but Fas, DR4 and DR5 are not. Additionally, we demonstrated that (i) the p42(mapk/erk2)-dependent phosphorylation of CD120a and DR3 occurred on Ser and Thr residues, (ii) p42(mapk/erk2) phosphorylated residues located in the membrane proximal regions but not the death domains of CD120a and DR3, (iii) Ser 253 is a preferred site of phosphorylation on CD120a, and (iv) the p42(mapk/erk2)-dependent phosphorylation of the DR3 cytoplasmic domain occurred exclusively at non-p42/44(mapk/erk2/1) consensus sites. These findings suggest that human death receptors segregate into two groups along lines of phylogeny with respect to Ser/Thr phosphorylation by p42(mapk/erk2).

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