Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
Article Abstract:
The crystal structure of an AB'C heterotrimeric protein phosphatase 2A (PP2A) holoenzyme reveals that the HEAT repeats of the scaffold A subunit form a horseshoe-shaped fold, holding the catalytic C and regulatory B' subunits together on the same side. The methylated carboxy-terminal tail of C subunit interacts with a highly negatively charged region at the interface between A and B' subunits, indicating that the C-terminal carboxyl methylation of the C subunit advances B' subunit recruitment by neutralizing charge repulsion.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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Phosphoinositides in cell regulation and membrane dynamics
Article Abstract:
The role of inositol phospholipids which play a fundamental part in controlling membrane-cytosol interfaces and act as constitutive signals that help define organelle identity is reviewed. Their functions, besides classical signal transduction at the cell surface, include regulation of membrane traffic, the cytoskeleton, nuclear events and the permeability and transport functions of membranes.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
Article Abstract:
The protein named Ciona intestinalis voltage sensors containing phosphatase, displays channel like gating currents and directly translates changes in membrane potential into the turnover of phosphoinositides. It is demonstrated that voltage sensing can function beyond channel proteins and thus more ubiquitously.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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