Novel protein interactors of urokinase-type plasminogen activator receptor
Copyright policy )Novel protein interactors of urokinase-type plasminogen activator receptor
The urokinase-type plasminogen activator receptor (uPAR) has been implicated in tumor growth and metastasis. The crystal structure of uPAR revealed that the external surface is largely free to interact with a number of proteins. Additionally, due to absence of an intracellular cytoplasmic protein domain, many of the biological functions of uPAR necessitate interactions with other proteins. Here, we used yeast two-hybrid screening of breast cancer cDNA library to identify hSpry1 and HAX1 proteins as putative candidate proteins that interact with uPAR bait constructs. Interaction between these two candidates and uPAR was confirmed by GST-pull down, co-immunoprecipitation assays and confocal microscopy. These novel interactions that have been identified may also provide further evidence that uPAR can interact with a number of other proteins which may influence a range of biological functions.
- UNSW Sydney Australia
- St George Hospital Australia
- University of Newcastle Australia Australia
yeast two-hybrid, HAX1, Membrane Proteins, Breast Neoplasms, 612, Phosphoproteins, Cell Line, Neoplasm Proteins, Receptors, Urokinase Plasminogen Activator, breast cancer, protein–protein interaction, Cell Line, Tumor, Two-Hybrid System Techniques, Humans, Immunoprecipitation, Female, hSpry1, uPAR, Adaptor Proteins, Signal Transducing, Gene Library
yeast two-hybrid, HAX1, Membrane Proteins, Breast Neoplasms, 612, Phosphoproteins, Cell Line, Neoplasm Proteins, Receptors, Urokinase Plasminogen Activator, breast cancer, protein–protein interaction, Cell Line, Tumor, Two-Hybrid System Techniques, Humans, Immunoprecipitation, Female, hSpry1, uPAR, Adaptor Proteins, Signal Transducing, Gene Library
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