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Mutual inhibition between PTEN and PIP3 generates bistability for polarity in motile cells
by
Ueda, Masahiro
, Matsuoka, Satomi
in
14
/ 14/19
/ 14/63
/ 631/57/2265
/ 631/80/84/1372
/ 631/80/86/2364
/ Binding sites
/ Binding Sites - genetics
/ Bistability
/ Cell Compartmentation - physiology
/ Cell Membrane - enzymology
/ Cell Membrane - metabolism
/ Cell Movement - physiology
/ Cell Polarity - physiology
/ Chemotaxis - physiology
/ Cyclic AMP - pharmacology
/ Decision making
/ Dictyostelium - cytology
/ Dictyostelium - enzymology
/ Dictyostelium - genetics
/ Enrichment
/ Humanities and Social Sciences
/ Kinetics
/ Lateral diffusion
/ Localization
/ Membranes
/ Models, Biological
/ multidisciplinary
/ Mutation
/ Phosphatidylinositol
/ Phosphatidylinositol 3,4,5-triphosphate
/ Phosphatidylinositol Phosphates - metabolism
/ Polarity
/ Protein Binding - drug effects
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - metabolism
/ PTEN Phosphohydrolase - chemistry
/ PTEN Phosphohydrolase - genetics
/ PTEN Phosphohydrolase - metabolism
/ PTEN protein
/ Science
/ Science (multidisciplinary)
/ Separation
/ Signal Transduction - physiology
2018
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Mutual inhibition between PTEN and PIP3 generates bistability for polarity in motile cells
by
Ueda, Masahiro
, Matsuoka, Satomi
in
14
/ 14/19
/ 14/63
/ 631/57/2265
/ 631/80/84/1372
/ 631/80/86/2364
/ Binding sites
/ Binding Sites - genetics
/ Bistability
/ Cell Compartmentation - physiology
/ Cell Membrane - enzymology
/ Cell Membrane - metabolism
/ Cell Movement - physiology
/ Cell Polarity - physiology
/ Chemotaxis - physiology
/ Cyclic AMP - pharmacology
/ Decision making
/ Dictyostelium - cytology
/ Dictyostelium - enzymology
/ Dictyostelium - genetics
/ Enrichment
/ Humanities and Social Sciences
/ Kinetics
/ Lateral diffusion
/ Localization
/ Membranes
/ Models, Biological
/ multidisciplinary
/ Mutation
/ Phosphatidylinositol
/ Phosphatidylinositol 3,4,5-triphosphate
/ Phosphatidylinositol Phosphates - metabolism
/ Polarity
/ Protein Binding - drug effects
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - metabolism
/ PTEN Phosphohydrolase - chemistry
/ PTEN Phosphohydrolase - genetics
/ PTEN Phosphohydrolase - metabolism
/ PTEN protein
/ Science
/ Science (multidisciplinary)
/ Separation
/ Signal Transduction - physiology
2018
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Mutual inhibition between PTEN and PIP3 generates bistability for polarity in motile cells
by
Ueda, Masahiro
, Matsuoka, Satomi
in
14
/ 14/19
/ 14/63
/ 631/57/2265
/ 631/80/84/1372
/ 631/80/86/2364
/ Binding sites
/ Binding Sites - genetics
/ Bistability
/ Cell Compartmentation - physiology
/ Cell Membrane - enzymology
/ Cell Membrane - metabolism
/ Cell Movement - physiology
/ Cell Polarity - physiology
/ Chemotaxis - physiology
/ Cyclic AMP - pharmacology
/ Decision making
/ Dictyostelium - cytology
/ Dictyostelium - enzymology
/ Dictyostelium - genetics
/ Enrichment
/ Humanities and Social Sciences
/ Kinetics
/ Lateral diffusion
/ Localization
/ Membranes
/ Models, Biological
/ multidisciplinary
/ Mutation
/ Phosphatidylinositol
/ Phosphatidylinositol 3,4,5-triphosphate
/ Phosphatidylinositol Phosphates - metabolism
/ Polarity
/ Protein Binding - drug effects
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - metabolism
/ PTEN Phosphohydrolase - chemistry
/ PTEN Phosphohydrolase - genetics
/ PTEN Phosphohydrolase - metabolism
/ PTEN protein
/ Science
/ Science (multidisciplinary)
/ Separation
/ Signal Transduction - physiology
2018
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Mutual inhibition between PTEN and PIP3 generates bistability for polarity in motile cells
Journal Article
Mutual inhibition between PTEN and PIP3 generates bistability for polarity in motile cells
2018
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Overview
Phosphatidylinositol 3,4,5-trisphosphate (PIP3) and PIP3 phosphatase (PTEN) are enriched mutually exclusively on the anterior and posterior membranes of eukaryotic motile cells. However, the mechanism that causes this spatial separation between the two molecules is unknown. Here we develop a method to manipulate PIP3 levels in living cells and used it to show PIP3 suppresses the membrane localization of PTEN. Single-molecule measurements of membrane-association and -dissociation kinetics and of lateral diffusion reveal that PIP3 suppresses the PTEN binding site required for stable PTEN membrane binding. Mutual inhibition between PIP3 and PTEN provides a mechanistic basis for bistability that creates a PIP3-enriched/PTEN-excluded state and a PTEN-enriched/PIP3-excluded state underlying the strict spatial separation between PIP3 and PTEN. The PTEN binding site also mediates the suppression of PTEN membrane localization in chemotactic signaling. These results illustrate that the PIP3-PTEN bistable system underlies a cell’s decision-making for directional movement irrespective of the environment.
PIP3 and its phosphatase (PTEN) are enriched mutually exclusively on the anterior and posterior membranes of eukaryotic motile cells. Here authors manipulate PIP3 level and use single-molecule imaging to show that PIP3 suppresses the membrane localization of PTEN.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 14/63
/ Cell Compartmentation - physiology
/ Humanities and Social Sciences
/ Kinetics
/ Mutation
/ Phosphatidylinositol 3,4,5-triphosphate
/ Phosphatidylinositol Phosphates - metabolism
/ Polarity
/ Protein Binding - drug effects
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - metabolism
/ PTEN Phosphohydrolase - chemistry
/ PTEN Phosphohydrolase - genetics
/ PTEN Phosphohydrolase - metabolism
/ Science
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