Membrane association of the PTEN tumor suppressor: Electrostatic interaction with phosphatidylserine-containing bilayers and regulatory role of the C-terminal tail

The phosphatidylinositolphosphate phosphatase PTEN is the second most frequently mutated protein in human tumors. Its membrane association, allosteric activation and membrane dissociation are poorly understood. We recently reported PTEN binding affinities to membranes of different compositions (Shen...

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Veröffentlicht in:	Journal of structural biology 2012-12, Vol.180 (3), p.394-408
Hauptverfasser:	Shenoy, Siddharth S., Nanda, Hirsh, Lösche, Mathias
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites C2 domain Humans Lipid Bilayers - chemistry Molecular Dynamics Simulation Neutron Diffraction Phosphatidylcholines - chemistry Phosphatidylserine Phosphatidylserines - chemistry PI3K pathway Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Protein–membrane interaction PTEN phosphatase PTEN Phosphohydrolase - chemistry Scattering, Small Angle Static Electricity
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