PTEN公司
磷酸化
苏氨酸
生物
突变体
癌症研究
细胞生物学
丝氨酸
生物化学
基因
信号转导
PI3K/AKT/mTOR通路
作者
Tatyana Tolkacheva,Manoranjan Boddapati,Anthony Sanfiz,Kunihiro Tsuchida,Alec C. Kimmelman,Andrew T. Chan
出处
期刊:PubMed
日期:2001-07-01
卷期号:61 (13): 4985-9
被引量:37
摘要
We have reported previously that the PTEN COOH-terminal 33 amino acids play a role in the maintenance of PTEN protein stability (Tolkacheva and Chan, Oncogene, 19: 680-689, 2000). By site-directed mutagenesis, we identified two threonine residues within this COOH-terminal region at codon 382 and 383 that may be targets for phosphorylation events. Interestingly, PTEN mutants rendered phosphorylation-incompetent at these two sites, T382A/T383A, and were found to have drastically reduced expression in cultured cells. The enhanced degradation of PTEN was most likely mediated by the proteosome-dependent pathway, we have evidence that PTEN was polyubiquitinated. More interestingly, the non-phosphorylated forms of PTEN displayed significantly greater binding affinity than the wild-type protein to a previously identified PTEN interacting partner, MAGI-2/ARIP1. On the basis of all these data, we propose that PTEN recruitment to the cell-cell junction may be regulated through the phosphorylation of its COOH terminus.
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