Helps N R, Barker H M, Elledge S J, Cohen P T
Department of Biochemistry, The University, Dundee, Scotland, UK.
FEBS Lett. 1995 Dec 27;377(3):295-300. doi: 10.1016/0014-5793(95)01347-4.
The p53 binding protein, termed p53BP2, was identified as a protein interacting with protein phosphatase 1 (PP1) in the yeast two hybrid system. The interaction was confirmed by co-immunoprecipitation of p53BP2 with epitope-tagged PP1 in vitro. The p53BP2-PP1 complex was stable to NaCl at concentrations which dissociate the p53-p53BP2 complex, and the binding of PP1 and p53 to p53BP2 was mutually exclusive. The region required for interaction with PP1 was shown to be contained within amino acids 297-431 of p53BP2, which includes two ankyrin repeats. The phosphorylase phosphatase activity of PP1 was inhibited by p53BP2 at nanomolar concentrations. These results suggest that PP1 may be involved in dephosphorylation and regulation of p53 through interaction with p53BP2.
一种名为p53BP2的p53结合蛋白,在酵母双杂交系统中被鉴定为与蛋白磷酸酶1(PP1)相互作用的蛋白。通过在体外对带有表位标签的PP1与p53BP2进行共免疫沉淀,证实了这种相互作用。p53BP2-PP1复合物在能使p53-p53BP2复合物解离的NaCl浓度下是稳定的,并且PP1和p53与p53BP2的结合是相互排斥的。已表明与PP1相互作用所需的区域包含在p53BP2的第297-431位氨基酸内,其中包括两个锚蛋白重复序列。在纳摩尔浓度下,p53BP2可抑制PP1的磷酸化酶磷酸酶活性。这些结果表明,PP1可能通过与p53BP2相互作用参与p53的去磷酸化和调控。