MXI2, A MITOGEN-ACTIVATED PROTEIN-KINASE THAT RECOGNIZES AND PHOSPHORYLATES MAX PROTEIN

Citation
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
Citations number
35
Categorie Soggetti
Multidisciplinary Sciences
ISSN journal
00278424
Volume
92
Issue
23
Year of publication
1995
Pages
10531 - 10534
Database
ISI
SICI code
0027-8424(1995)92:23<10531:MAMPTR>2.0.ZU;2-8
Abstract
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.