Tyrosine phosphorylation-independent nuclear translocation of a Dictyostelium STAT in response to DIF signaling

被引：69

作者：

Fukuzawa, M ^{[1
]}

Araki, T ^{[1
]}

Adrian, I ^{[1
]}

Williams, JG ^{[1
]}

机构：

[1] Univ Dundee, Sch Life Sci, Dundee DD1 5EH, Scotland

来源：

MOLECULAR CELL | 2001年 / 7卷 / 04期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/S1097-2765(01)00222-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We describe a Dictyostelium STAT, Dd-STATc, which regulates the speed of early development and the timing of terminal differentiation. Dd-STATc also functions as a repressor, which directs graded expression of the ecmA gene in different prestalk cell populations. Developing Dictyostelium cells produce a chlorinated hexaphenone, DIF, which directs prestalk cell differentiation. Dd-STATc is tyrosine phosphorylated, dimerizes, and translocates to the nucleus when cells are exposed to DIF. Surprisingly, however, SH2 domain-phosphotyrosine interaction is not necessary for the DIF-induced nuclear translocation of Dd-STATc. In this respect, Dd-STATc activation resembles several recently described, noncanonical mammalian STAT signaling processes. We show instead that DIF mediates nuclear translocation via sequences located in the divergent, N-terminal half of the Dd-STATc molecule.

引用

页码：779 / 788

页数：10

共 41 条

[1] Developmentally and spatially regulated activation of a Dictyostelium STAT protein by a serpentine receptor [J].