Journal article
Plant development: regulation by protein degradation
Science (American Association for the Advancement of Science), Vol.297(5582), pp.793-797
08/02/2002
Handle:
https://hdl.handle.net/2376/109331
PMID: 12161644
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.
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Details
- Title
- Plant development: regulation by protein degradation
- Creators
- Hanjo Hellmann - Molecular Cell and Developmental Biology, University of Texas, Austin, TX 78712, USAMark Estelle
- Publication Details
- Science (American Association for the Advancement of Science), Vol.297(5582), pp.793-797
- Academic Unit
- Biological Sciences, School of
- Publisher
- United States
- Grant note
- GM43644 / NIGMS NIH HHS
- Identifiers
- 99900547054101842
- Language
- English
- Resource Type
- Journal article