The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor

Article Abstract:

Research reveals that the tumor suppressor protein, ING2, is a nuclear phosphoinositide receptor and contains a plant homeodomain (PHD) finger. Data indicate that the PHD fingers bind to phosphoinositides including phosphatidylinositol 5-phosphate with which it interacts to regulate ING2 activation of p53 and p53-dependent apoptotic pathways.

France, DNA damage, Cellular control mechanisms, Cell regulation, Enzyme activation

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Phoxy lipids: revealing PX domains as phosphoinositide binding modules

Article Abstract:

Results suggest that the PX domain is a phosphoinositide-specific binding module involved in the targeting of proteins to specific cellular membranes in eukaryotic organisms. Structure-function studies show that PX domain exhibits lipid-binding specificity with individual PX domains recognizing different phosphoinositides.

Biological transport, Lipids

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Identification of a bacterial type III effector family with G protein mimicry functions

Article Abstract:

The identification of a 24 member effector protein family found in pathogens including Salmonella, Shigella, and enteropathogenic E. coli are reported. The report suggests for the first time that IpgB1, IpgB2, and Map function by a common molecular mechanism as functional mimics of distinct Rho family GTPases.

Science & research, Research, Salmonella, G proteins, Bacterial proteins, Chemical properties, Shigella

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