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A mutant form of PTEN linked to autism.

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A mutant form of PTEN linked to autism.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gericke, Arne Li, Li Ross, Alonzo H. Daou, Marie-Claire Munson, Mary Redfern, Roberta E.
Description	Country affiliation: United States Author Affiliation: Redfern RE ( Chemistry Department, Kent State University, Kent, Ohio 44242, USA.)
Abstract	The tumor suppressor, phosphatase, and tensin homologue deleted on chromosome 10 (PTEN), is a phosphoinositide (PI) phosphatase specific for the 3-position of the inositol ring. PTEN has been implicated in autism for a subset of patients with macrocephaly. Various studies identified patients in this subclass with one normal and one mutated PTEN gene. We characterize the binding, structural properties, activity, and subcellular localization of one of these autism-related mutants, H93R PTEN. Even though this mutation is located at the phosphatase active site, we find that it affects the functions of neighboring domains. H93R PTEN binding to phosphatidylserine-bearing model membranes is 5.6-fold enhanced in comparison to wild-type PTEN. In contrast, we find that binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P(2)) model membranes is 2.5-fold decreased for the mutant PTEN in comparison to wild-type PTEN. The structural change previously found for wild-type PTEN upon interaction with PI(4,5)P(2), is absent for H93R PTEN. Consistent with the increased binding to phosphatidylserine, we find enhanced plasma membrane association of PTEN-GFP in U87MG cells. However, this enhanced plasma membrane association does not translate into increased PI(3,4,5)P(3) turnover, since in vivo studies show a reduced activity of the H93R PTEN-GFP mutant. Because the interaction of PI(4,5)P(2) with PTEN's N-terminal domain is diminished by this mutation, we hypothesize that the interaction of PTEN's N-terminal domain with the phosphatase domain is impacted by the H93R mutation, preventing PI(4,5)P(2) from inducing the conformational change that activates phosphatase activity.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.483
Journal	Protein Science
Issue Number	10
Volume Number	19
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2010-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Autistic Disorder Genetics Mutation Pten Phosphohydrolase Tumor Suppressor Proteins Amino Acid Substitution Enzymology Cell Line, Tumor Cell Membrane Metabolism Green Fluorescent Proteins Membrane Lipids Microscopy, Confocal Phosphatidylinositol 4,5-diphosphate Phosphatidylinositols Phosphatidylserines Protein Binding Recombinant Fusion Proteins Spectrophotometry, Infrared Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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