Phosphatidylinositol 3-Phosphate Induces the Membrane Penetration of the FYVE Domains of Vps27p and Hrs
| Autor: | Wonhwa Cho, Robert V. Stahelin, Karol S. Bruzik, Diana Murray, Karthikeyan Diraviyam, Fei Long |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins Protein Conformation Static Electricity Vesicular Transport Proteins Biology Biochemistry chemistry.chemical_compound Protein structure Phosphatidylinositol Phosphates Animals Phosphatidylinositol Molecular Biology Endosomal Sorting Complexes Required for Transport Phosphatidylinositol 3-phosphate Vesicle Cell Membrane Zinc Fingers Biological membrane Cell Biology Phosphoproteins Cell biology DNA-Binding Proteins Kinetics Membrane chemistry Mutation FYVE domain Drosophila Carrier Proteins Microtubule-Associated Proteins Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 277:26379-26388 |
| ISSN: | 0021-9258 |
| Popis: | The FYVE domain mediates the recruitment of proteins involved in membrane trafficking and cell signaling to phosphatidylinositol 3-phosphate (PtdIns(3)P)-containing membranes. To elucidate the mechanism by which the FYVE domain interacts with PtdIns(3)P-containing membranes, we measured the membrane binding of the FYVE domains of yeast Vps27p and Drosophila hepatocyte growth factor-regulated tyrosine kinase substrate and their mutants by surface plasmon resonance and monolayer penetration analyses. These measurements as well as electrostatic potential calculation show that PtdIns(3)P specifically induces the membrane penetration of the FYVE domains and increases their membrane residence time by decreasing the positive charge surrounding the hydrophobic tip of the domain and causing local conformational changes. Mutations of hydrophobic residues located close to the PtdIns(3)P-binding pocket or an Arg residue directly involved in PtdIns(3)P binding abrogated the penetration of the FYVE domains into the monolayer, the packing density of which is comparable with that of biological membranes and large unilamellar vesicles. Based on these results, we propose a mechanism of the membrane binding of the FYVE domain in which the domain first binds to the PtdIns(3)P-containing membrane by specific PtdIns(3)P binding and nonspecific electrostatic interactions, which is then followed by the PtdIns(3)P-induced partial membrane penetration of the domain. |
| Databáze: | OpenAIRE |
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