Regulation of PTEN binding to MAGI-2 by two putative phosphorylation sites at threonine 382 and 383

Tatyana Tolkacheva, Manoranjan Boddapati, Anthony Sanfiz, Alec C. Kimmelman, Andrew M.L. Chan, Kunihiro Tsuchida

Research output: Contribution to journalArticlepeer-review

114 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)4985-4989
Number of pages5
JournalCancer Research
Issue number13
Publication statusPublished - 01-07-2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Oncology
  • Cancer Research


Dive into the research topics of 'Regulation of PTEN binding to MAGI-2 by two putative phosphorylation sites at threonine 382 and 383'. Together they form a unique fingerprint.

Cite this