Zervos A S, Faccio L, Gatto J P, Kyriakis J M, Brent R
Cutaneous Biology Research Center, Massachusetts General Hospital/Harvard Medical School, Charlestown, USA.
Proc Natl Acad Sci U S A. 1995 Nov 7;92(23):10531-4. doi: 10.1073/pnas.92.23.10531.
We describe Mxi2, a human protein that interacts with Max protein, the heterodimeric partner of the Myc oncoprotein. Mxi2 encodes a 297-residue protein whose sequence indicates that it is related to extracellular signal-regulated kinases (ERK protein kinases). Mxi2 in yeast interacts with Max and with the C terminus of c-Myc. Mxi2 phosphorylates Max both in vitro and in vivo. The Mxi2 putative substrate recognition region has sequence similarity to the helix-loop-helix region in Max and c-Myc, suggesting that substrate recognition might be mediated via this motif. Phosphorylation by Mxi2 may affect the ability of Max to oligomerize with itself and its partners, bind DNA, or regulate gene expression.
我们描述了Mxi2，一种与Max蛋白相互作用的人类蛋白质，Max蛋白是Myc癌蛋白的异二聚体伴侣。Mxi2编码一种由297个氨基酸残基组成的蛋白质，其序列表明它与细胞外信号调节激酶（ERK蛋白激酶）相关。酵母中的Mxi2与Max以及c-Myc的C末端相互作用。Mxi2在体外和体内均可使Max磷酸化。Mxi2的假定底物识别区域与Max和c-Myc中的螺旋-环-螺旋区域具有序列相似性，这表明底物识别可能是通过该基序介导的。Mxi2介导的磷酸化可能会影响Max自身及其伴侣寡聚化、结合DNA或调节基因表达的能力。
