Crystal structure of GLUE complexed to ubiquitin published in Nature Structural & Molecular Biology

T. Slagsvold
Thomas Slagsvold, a postdoc in Harald Stenmark’s lab has previously identified a novel ubiquitin- and phosphoinositide binding domain, called GLUE. This identification was in collaboration with Rein Aasland at the University of Bergen and Soichi Wakatuki’s group at the Structural Biology Research Center in Ibaraki, Japan. In a continued collaboration with Wakatsuki’s group the crystal structure of the GLUE domain complexed to ubiquitin has now been solved. The structure is published in a recent issue of the prestigious journal "Nature Structural & Molecular Biology" (impact factor 12,19).
The GLUE domain is found in the endosomal protein Eap45, which is involved in sorting of ubiquitinated membrane proteins from endosomes to lysosomes. An article from the Stenmark group - entitled "Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain", with Slagsvold as first writer, was selected "JBC Paper of the week" last year - click here to read more.

The structure shows how the GLUE domain binds to the hydrophobic patch of ubiquitin and reveals that the ubiquitin- and phosphoinositide-binding sites of the GLUE domains are separate.

(click to enlarge)
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