FASEB Summer Conference: Ubiquitin and Intracellular Protein Degradation to be held July 31- Aug. 5, 1999, in Saxton's River, VT.

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PickartThe conference "Ubiquitin and Intracellular Protein Degradation" will be held from July 31 through August 5, 1999, at the Conference Center of the Vermont Academy in Saxton's River, VT. This meeting is sponsored by the Federation of the American Societies for Experimental Biology (FASEB). It has been held biennially since 1989. It is the only regularly-held international meeting devoted to the biology and biochemistry of ubiquitin. This award provides partial funding for the 1999 conference.The conserved protein ubiquitin is essential in eukaryotes. The biological functions of ubiquitin are mediated by its covalent attachment, through its C-terminal carboxyl group, to lysine residues of cellular proteins. The best-understood function of ubiquitin is that of a signal which targets proteins for ATP-dependent degradation by the 26S proteasome. In this novel proteolytic pathway, substrate selection and the chemical catalysis of substrate hydrolysis are carried out by separate enzymes, allowing diverse substrates to be recognized and degraded with high selectivity and efficiency. The proteasome is the paradigmatic example of a universally distributed set of ATP-dependent proteases which feature sequestered active sites and a necessity for the coupling of substrate unfolding to proteolysis. By setting the levels of key regulatory proteins, the ubiquitin--proteasome degradation pathway controls fundamental intracellular processes, including the progression of the cell cycle. Besides ubiquitin, eukaryotes possess a family of ubiquitin-like proteins which undergo a metabolism parallel to, but distinct from, that of ubiquitin. These molecules appear to function as covalent signals which target their substrates to specific locations within the cell. The presentations and discussions in the 1999 conference will substantially advance the understanding of the functions of ubiquitin and its homologs.