Griswold-Prenner I, Kamibayashi C, Maruoka E M, Mumby M C, Derynck R
Department of Growth and Development, University of California at San Francisco, San Francisco, California 94143-0640, USA.
Mol Cell Biol. 1998 Nov;18(11):6595-604. doi: 10.1128/MCB.18.11.6595.
We have previously shown that a WD-40 repeat protein, TRIP-1, associates with the type II transforming growth factor beta (TGF-beta) receptor. In this report, we show that another WD-40 repeat protein, the Balpha subunit of protein phosphatase 2A, associates with the cytoplasmic domain of type I TGF-beta receptors. This association depends on the kinase activity of the type I receptor, is increased by coexpression of the type II receptor, which is known to phosphorylate and activate the type I receptor, and allows the type I receptor to phosphorylate Balpha. Furthermore, Balpha enhances the growth inhibition activity of TGF-beta in a receptor-dependent manner. Because Balpha has been characterized as a regulator of phosphatase 2A activity, our observations suggest possible functional interactions between the TGF-beta receptor complex and the regulation of protein phosphatase 2A.
我们先前已表明,一种WD-40重复蛋白TRIP-1与II型转化生长因子β(TGF-β)受体相关联。在本报告中,我们表明另一种WD-40重复蛋白,即蛋白磷酸酶2A的Bα亚基,与I型TGF-β受体的胞质结构域相关联。这种关联依赖于I型受体的激酶活性,通过已知可磷酸化并激活I型受体的II型受体的共表达而增强,并且使得I型受体能够磷酸化Bα。此外,Bα以受体依赖的方式增强TGF-β的生长抑制活性。由于Bα已被表征为磷酸酶2A活性的调节剂,我们的观察结果提示了TGF-β受体复合物与蛋白磷酸酶2A调节之间可能存在的功能相互作用。