Woodgett J R
Ludwig Institute for Cancer Research, London, UK.
Trends Biochem Sci. 1991 May;16(5):177-81. doi: 10.1016/0968-0004(91)90071-3.
A ubiquitous protein-serine kinase, initially implicated in glycogen regulation, has surfaced unexpectedly in the fields of nuclear oncogenes and fruitfly development. This unusual linkage may reflect the role of this kinase in phosphorylating proteins normally activated by dephosphorylation, thus providing a priming function. Loss of such a primer would result in constitutive activation of substrates, a scenario concordant with the dramatic and pleiotropic phenotype observed in Drosophila null mutants.
一种普遍存在的蛋白丝氨酸激酶，最初被认为与糖原调节有关，却意外地出现在核癌基因和果蝇发育领域。这种不同寻常的联系可能反映了该激酶在使通常通过去磷酸化激活的蛋白质磷酸化方面的作用，从而提供一种引发功能。失去这样一种引发物会导致底物的组成型激活，这一情况与在果蝇基因敲除突变体中观察到的显著且多效性的表型相一致。
