Tyrosine phosphorylation-independent nuclear translocation of a Dictyostelium STAT in response to DIF signaling
Tyrosine phosphorylation-independent nuclear translocation of a Dictyostelium STAT in response to DIF signaling
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DOI:
10.1016/s1097-2765(01)00222-2
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发表时间:
2001-04-01
期刊:
影响因子:
16
通讯作者:
Williams, JG
中科院分区:
文献类型:
--
作者:
Fukuzawa, M;Araki, T;Williams, JG
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.