Functional form of Caveolin-1 is necessary for the assembly of α-hemolysin

The assembly of α-HL was shown to rapidly progress upon its interaction with Caveolin-1. Treatment of A431 cells with α-HL has resulted in clustering of Caveolin-1 at cell–cell contacts. Consistent with this observation, α-HL mutants devoid of assembly property have not induced the clustering of Cav...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2004-11, Vol.324 (3), p.1130-1136
Main Authors: Vijayvargia, Ravi, Suresh, C.G., Krishnasastry, Musti V.
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Bacterial Toxins - chemistry
Bacterial Toxins - genetics
Caveolin 1
Caveolins - chemistry
Caveolins - metabolism
Cell Line, Tumor
Cell Membrane - metabolism
Cholesterol - metabolism
Down-Regulation
Electrophoresis, Polyacrylamide Gel
Functional Caveolin-1
Hemolysin Proteins - chemistry
Hemolysin Proteins - genetics
Heptameric assembly
Humans
Immunoprecipitation
Kinetics
Membrane penetration
Methionine - chemistry
Microscopy, Fluorescence
Models, Molecular
Mutation
Nystatin - pharmacology
Peptides - chemistry
Protein Binding
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Protein–protein interactions
Time Factors
α-Hemolysin
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Summary:The assembly of α-HL was shown to rapidly progress upon its interaction with Caveolin-1. Treatment of A431 cells with α-HL has resulted in clustering of Caveolin-1 at cell–cell contacts. Consistent with this observation, α-HL mutants devoid of assembly property have not induced the clustering of Caveolin-1. While cholesterol depletion of A431 cells completely arrests the assembly of α-HL, chelation of membrane cholesterol results in its retarded assembly. Interestingly, HT29 cells, with low Caveolin-1 levels, are resistant to α-HL attack. Clustering of Caveolin-1, as seen in case of A431 cells, was readily observed in case of HT29 cells transfected with Caveolin-1 construct, thus overexpressing the full length Caveolin-1, upon α-HL treatment. A model was constructed to visualize the interactions between α-HL and Caveolin-1 which suggests that facile penetration of α-HL’s β-barrel might occur through protein–protein interactions with the surrounding 7 α-helices of Caveolin-1.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.09.164