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Abstract
Many aspects of eukaryotic development depend on regulated protein degradation by the ubiquitin-proteasome pathway. This highly conserved pathway promotes covalent attachment of ubiquitin to protein substrates through the sequential action of three enzymes called a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-protein ligase (E3). Most ubiquitinated proteins are then targeted for degradation by the 26S proteasome. Recent studies have also shown that the ubiquitin-related protein RUB/Nedd8 and the proteasome-related COP9 signalosome complex cooperate with the ubiquitin-proteasome pathway to promote protein degradation. Most of these components are conserved in all three eukaryotic kingdoms. However, the known targets of the pathway in plants, and the developmental processes they regulate, are specific to the plant kingdom.
↵* Present address: Institut für Angewandte Genetik, Molekulare Entwicklungsbiologie der Pflanzen, Albrecht-Thaer Weg 7, 14195 Berlin, Germany.
↵† Present address: Myers Hall, Indiana University, 915 East Third Street, Bloomington, IN 47405, USA.
↵‡ To whom correspondence should be addressed. E-mail: mestelle{at}bio.indiana.edu
