|Title:||Nuclear Extracellular Signal-Regulated Kinase 2 Phosphorylates P53 at Thr 55 in Response to Doxorubicin||Authors:||CHENG, ANN-LII
|Keywords:||ERK2;p53;phosphorylation;anticancer drugs;ACTIVATED PROTEIN- KINASES;XENOPUS EGG EXTRACTS||Issue Date:||2001||Journal Volume:||v.284||Journal Issue:||886||Start page/Pages:||-||Source:||BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS||Abstract:||
In this study, we showed that nuclear ERK2 phosphorylates p 53 at Thr55 in response to doxorubicin. p53 was found to physically interact with ERK2 as evidenced by Western blotting of ERK2 coimmunoprecipitated complex. The gene fragment encoded for N-terminal 68 amino acids was subcloned and fused with 6-His. Each serine or threonine site in this fragment, the possible phosyphorylation site, was mutated to alanine. The recombinant proteins were used as substrates in ERK2 kinase assay. The results show that ERK2 phosphorylated p53 at Thr55. Further, electromobility shift assay showed that the phosphorylation of p53 by nuclear ERK2 was closely related to the transactivating activity of p53. These findings suggest that ERK2 may play a role in response to DNA damage via interaction with p 53. (C) 2001 Academic Press.
|Appears in Collections:||醫學系|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.