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The PTEN Tumor Suppressor Forms Homodimers in Solution



Frank Heinrich, Srinivas Chakravarthy, Hirsh Nanda, Antonella Papa, Pier Paolo Pandolfi, Alonzo H. Ross, Rakesh K. Harishchandra, Arne Gericke, Peter M. Loesche


The PTEN tumor suppressor exerts phosphatase activity on PI(3,4,5)P3 in the plasma membrane and was recently reported to dimerize in cell models. Here we show that PTEN forms homodimers in vitro and determine a structural model of the complex from SAXS and Rosetta docking studies. PTEN's C-terminal tail is disordered on the monomer but presumable well-folded on the dimer, shedding new light on its regulatory role.


PI3K/Akt pathway, PTEN phosphatase, dimer structure, SAXS, protein docking


Heinrich, F. , Chakravarthy, S. , , H. , Papa, A. , , P. , , A. , , R. , Gericke, A. and Loesche, P. (2015), The PTEN Tumor Suppressor Forms Homodimers in Solution, Structure, [online], (Accessed July 17, 2024)


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Created August 21, 2015, Updated February 19, 2017