As. Zervos et al., MXI2, A MITOGEN-ACTIVATED PROTEIN-KINASE THAT RECOGNIZES AND PHOSPHORYLATES MAX PROTEIN, Proceedings of the National Academy of Sciences of the United Statesof America, 92(23), 1995, pp. 10531-10534
We describe Mxi2, a human protein that interacts with Max protein, the
heterodimeric partner of the Myc oncoprotein. Mxi2 encodes a 297-resi
due protein whose sequence indicates that it is related to extracellul
ar signal-regulated kinases (ERK protein kinases). Mxi2 in yeast inter
acts with Max and with the C terminus of c-Myc. Mxi2 phosphorylates Ma
x both in vitro and in vivo. The Mxi2 putative substrate recognition r
egion has sequence similarity to the helix-loop-helix region in Max an
d c-Myc, suggesting that substrate recognition might be mediated via t
his motif. Phosphorylation by Mxi2 may affect the ability of Max to ol
igomerize with itself and its partners, bind DNA, or regulate gene exp
ression.