Document Detail

Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs.
MedLine Citation:
PMID:  12006563     Owner:  NLM     Status:  MEDLINE    
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.
Robert V Stahelin; Fei Long; Karthikeyan Diraviyam; Karol S Bruzik; Diana Murray; Wonhwa Cho
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.     Date:  2002-05-10
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Jul 
Date Detail:
Created Date:  2002-07-15     Completed Date:  2002-09-06     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  26379-88     Citation Subset:  IM    
Department of Chemistry, University of Illinois, Chicago, Illinois 60607, USA.
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MeSH Terms
Carrier Proteins / metabolism*
Cell Membrane / metabolism*
DNA-Binding Proteins / metabolism*
Endosomal Sorting Complexes Required for Transport
Models, Molecular
Phosphatidylinositol Phosphates / genetics,  pharmacology*
Phosphoproteins / metabolism*
Protein Conformation
Saccharomyces cerevisiae Proteins*
Static Electricity
Transcription Factors / metabolism*
Vesicular Transport Proteins*
Zinc Fingers
Grant Support
Reg. No./Substance:
0/Carrier Proteins; 0/DNA-Binding Proteins; 0/Endosomal Sorting Complexes Required for Transport; 0/FYCO1 protein, human; 0/Phosphatidylinositol Phosphates; 0/Phosphoproteins; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factors; 0/VPS27 protein, S cerevisiae; 0/Vesicular Transport Proteins; 0/hepatocyte growth factor-regulated tyrosine kinase substrate; 0/phosphatidylinositol 3-phosphate

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