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New regulatory mechanism discovered in cell system for eliminating unneeded proteins
Date:8/10/2012

ion process, a small protein is passed from one enzyme to the next like a baton in a relay race until it reaches a protein complex known as the cullin RING ligase. There, the small protein is transferred to a waiting target protein, marking it for destruction.

In this study, researchers showed that Glomulin disrupts ubiquitination by "glomming" onto and masking the spot on the cullin RING ligase where the tagging process is completed. The binding site is on the RBX1 protein, a component of the cullin RING ligase. While Glomulin derives its name from the disease, researchers showed the name also aptly describes Glomulin's molecular function.

The study builds on earlier work from the laboratory of James DeCaprio, M.D., of the Dana-Farber Cancer Institute, Boston. DeCaprio, a coauthor of this study, and his colleagues reported that Glomulin regulates cullin RING ligases by binding to the RBX1 protein. They also reported that Glomulin does not bind to the related RBX2 protein.

In this latest study, St. Jude scientists used X-ray crystallography to determine the structures involved in Glomulin's interaction with RBX1 and another component of the cullin RING ligase. "This was one of those 'ah-ha' moments," Schulman said. "Seeing the structure told us almost immediately how Glomulin disrupts the ubiquitination process."

Additional tests showed that Glomulin binds tightly to the surface of the RBX1 protein. The binding prevents the enzyme carrying the kiss-of-death protein tag from delivering its cargo. The structure also suggests how Glomulin mutations associated with glomuvenous malformations prevent the protein from binding to RBX1.

Researchers showed that Glomulin disrupts ubiquitination by binding to the same spot on the cullin RING ligase where the enzyme carrying the ubiquitin protein must bind to complete the process. The location is on the RBX1 protein, which is part of the larger protein complex.

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Contact: Carrie Strehlau
media@stjude.org
901-595-2295
St. Jude Children's Research Hospital
Source:Eurekalert

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