beta(1) integrin binds the 16-kDa subunit of vacuolar H(+)-ATPase at a site important for human papillomavirus E5 and platelet-derived growth factor signaling
| Autor: | Alan G. Wildeman, Mhairi A. Skinner |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Vacuolar Proton-Translocating ATPases
Recombinant Fusion Proteins Integrin Molecular Sequence Data Biology Biochemistry CD49c Collagen receptor Cell Line Focal adhesion Epitopes Tumor Cells Cultured Animals Humans Amino Acid Sequence Molecular Biology DNA Primers Platelet-Derived Growth Factor Base Sequence Integrin beta1 Cell Biology Oncogene Proteins Viral Molecular biology Precipitin Tests Cell biology Rats Transmembrane domain Proton-Translocating ATPases Integrin alpha M biology.protein Integrin beta 6 Signal transduction Protein Binding |
| Zdroj: | The Journal of biological chemistry. 274(33) |
| ISSN: | 0021-9258 |
| Popis: | Integrins mediate adhesive interactions between cells and the extracellular matrix, and play a role in cell migration, proliferation, differentiation, cytoskeletal organization, and signal transduction. We have identified an interaction between the beta(1) integrin and the 16-kDa subunit of vacuolar H(+)-ATPase (16K). This interaction was first isolated in a yeast two-hybrid screen and confirmed by coimmunoprecipitation and in in vitro binding assays using bacterially expressed proteins. Immunofluorescent studies performed in L6 myoblasts expressing both native and epitope-tagged 16K demonstrate co-localization with beta(1) integrin in focal adhesions. Deletion of the fourth of four transmembrane helices in 16K results in loss of interaction with beta(1) integrin in vitro and in the two-hybrid system, and less prominent staining in focal adhesions. This helix is also required for ligand-independent activation of platelet-derived growth factor-beta receptor signaling by the human papillomavirus E5 oncoprotein. Overexpression of 16K or expression of 16K lacking this helix alters the morphology of myoblasts and fibroblasts, suggesting that the interaction of 16K with integrins could be important for cell growth control. We also discuss the possible role 16K might play in integrin movement. |
| Databáze: | OpenAIRE |
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