'Ubiquitin and ubiquitin-like proteins' Poster

Protein ubiquitylation is a recognized signal for protein degradation.  However, it is increasingly realized that ubiquitin conjugation to proteins can be used for many other purposes, and there are many ubiquitin-like proteins that control the activities of proteins.  The central structural element of these post-translational modifications is the ubiquitin superfold and, as well as being small conjugatable protein modifiers, ubiquitin superfolds can be domains that are genetically built into much larger proteins.  An encompassing term for each of these structural folds is ‘ubiquiton’.  Ubiquitons have various functions, most of which are unrelated to protein degradation, and some ubiquitons have little homology to ubiquitin.  In the future, it is anticipated that numerous regulatory proteins will be found to be are conjugated to ubiquitons to enhance the specificity of protein interactions.

An attractive poster summarising much of the current knowledge concerning these important aspects of post-translational modification has been prepared as the result of a collaboration between Professor John Mayer's group at the University of Nottingham, BIOMOL International LP, and the Nature publishing group.  The poster supplements a review article by Welchman, R.L., Gordon, C. and Mayer, R.J. in the August 2005 issue of Nature Reviews Molecular Cell Biology.

A copy of this poster is available as a high resolution pdf file by clicking here or a hard copy may be requested directly here.

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