Identification of a Myosin VII-Talin Complex

Myosin VII (M7) plays a role in adhesion in both Dictyostelium and mammalian cells where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. The nature of this complex is not fully known, prompting a search for M7-binding proteins. C...

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Published inThe Journal of biological chemistry Vol. 280; no. 28; pp. 26557 - 26564
Main Authors Tuxworth, Richard I., Stephens, Stephen, Ryan, Zachary C., Titus, Margaret A.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.07.2005
American Society for Biochemistry and Molecular Biology
Subjects
Actins - chemistry
Animals
Cell Adhesion
Cell Membrane - metabolism
Centrifugation, Density Gradient
Cytoskeleton - metabolism
Detergents - pharmacology
Dictyostelium
Dictyostelium - metabolism
Green Fluorescent Proteins - metabolism
Humans
Immunoblotting
Immunoprecipitation
Myosins - chemistry
Plasmids - metabolism
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Protozoan Proteins - chemistry
Sucrose - pharmacology
Talin - chemistry
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Summary:Myosin VII (M7) plays a role in adhesion in both Dictyostelium and mammalian cells where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. The nature of this complex is not fully known, prompting a search for M7-binding proteins. Co-immunoprecipitation experiments reveal that Dictyostelium M7 (DdM7) interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. No additional proteins are observed in the immunoprecipitate, indicating that the interaction is direct. The N-terminal region of the DdM7 tail that lies between the region of predicted coil and the first MyTH4 domain is found to harbor the talinA binding site. Localization experiments reveal that talinA does not serve as a membrane receptor for DdM7 and vice versa. These findings reveal that talinA is a major DdM7 binding partner and suggest that their interaction induces a conformational change in each that, in combination with membrane receptor binding, promotes the assembly of a high avidity receptor complex essential for adhesion of the cell to substrata.
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ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M503699200