August 13, 2012 / Bio Valley BIOON /-In a new study, researchers at St. Jude Childrens Research Hospital in the United States discovered a disease associated with a rare vascular disease The defective gene allowed them to discover a mechanism involved in determining the fate of about a thousand proteins in the cell. This discovery helps people to gain a deeper understanding of the ubiquitin system, one of the most important regulatory systems in the body. Cells use the ubiquitin system to remove unwanted proteins. Such systemic problems are associated with cancer, infections and other diseases. The research was recently published online in the journal Molecular Cell.
The researchers demonstrated how a protein called glomerulin binds to a key component of this regulatory system. They not only confirmed the binding location of glomerulin, but also how this binding shuts down a biochemical cascade: this cascade reaction marks unwanted proteins in order to remove them.
In this study, the researchers found that glomerulin binds to the site of cullin-RING ubiquitin ligase (cullin RING ligase) and covers this site, thereby disrupting ubiquitination, of which cullin-RING Ubiquitin ligase completes the ubiquitin labeling process. The binding site of glomerulin is located on the RBX1 protein, which is a component of cullin-RING ubiquitin ligase.
In an earlier study, researcher James DeCaprio and his colleagues reported that glomerulin regulates cullin-RING ubiquitin ligase by binding to the RBX1 protein. They also reported that glomerular protein did not bind to RBX2 protein associated with RBX1 protein.
In this latest study, researchers at St. Jude Children ’s Research Hospital used X-ray crystallography to determine the structure involved in the interaction of glomerulin with another component of the RBX1 protein and cullin-RING ubiquitin ligase .
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Subsequent tests also showed that glomerulin tightly bound to the surface of RBX1 protein. This binding prevents cullin-RING ubiquitin ligases carrying ubiquitin tags from transporting ubiquitin. This structure also suggests how the glomerular protein mutations associated with glomuvenous malformation prevent this protein from binding to the RBX1 protein.
The cullin-RING ubiquitin ligase carrying the ubiquitin protein must bind to the RBX1 protein to complete the ubiquitination process. The researchers found that glomerulin binds to cullin-RING ubiquitin ligase, which binds to the same site on the RBX1 protein, thereby disrupting ubiquitination.
Dr. David Duda, the first author of the paper, said, "RBX1 protein potentially regulates thousands of different proteins in the cell. Glomerulin represents a new way to regulate this type of RBX1-related protein."
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