AVS 58th Annual International Symposium and Exhibition
    Biomaterial Interfaces Division Tuesday Sessions
       Session BI-TuA

Invited Paper BI-TuA7
Membrane Binding, Structure and Regulation of the PTEN Phosphatase

Tuesday, November 1, 2011, 4:00 pm, Room 105

Session: Protein-Membrane Interactions
Presenter: Matthias Lösche, Carnegie Mellon University and National Institute of Standards and Technology
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Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is an important regulatory protein and tumor suppressor that performs its phosphatase activity as an interfacial enzyme at the plasma membrane-cytoplasm boundary. Acting as an antagonist to phosphoinositide-3-kinase (PI3K) in cell signaling, it is deleted in many human cancers. Despite its importance in regulating the levels of the phosphatidylinositoltriphosphate PI(3,4,5)P3, there is little understanding of how PTEN binds to membranes, is activated and then acts as a phosphatase. The interaction of the protein with membranes is highly dynamic and is at least partially controlled by the in-plane fluidity of the bilayer. PTEN function requires multiple, lipid-specific interactions with the target membrane. These interactions regulate enzyme activity as well as lateral and subcellular distribution of the enzyme. From studies of the membrane association of PTEN under well-defined conditions in model systems, we report recent insights in the structural and functional basis for PTEN membrane binding and regulation.