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Biochem Biophys Res Commun. 2010 Sep 3;399(4):738-43. doi: 10.1016/j.bbrc.2010.08.010. Epub 2010 Aug 7.

Novel protein interactors of urokinase-type plasminogen activator receptor.

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Cancer Research Laboratories, Department of Surgery, St. George Hospital, University of New South Wales, Sydney, NSW 2217, Australia.


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.

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