@article {3095172,
	title = {Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue.},
	journal = {Nat Cell Biol},
	volume = {9},
	year = {2007},
	month = {2007 Apr},
	pages = {422-7},
	abstract = {Cells have quality-control mechanisms to recognize non-native protein structures and either help the proteins fold or promote their degradation. Ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s) work together to assemble polyubiquitin chains on misfolded or misassembled proteins, which are then degraded by the proteasome. Here, we find that Ubc7, a yeast E2, can itself undergo degradation when its levels exceed that of its binding partner Cue1, a transmembrane protein that tethers Ubc7 to the endoplasmic reticulum. Unassembled, and thus mislocalized, Ubc7 is targeted to the proteasome by Ufd4, a homologous to E6-AP C-terminus (HECT)-class E3. Ubc7 is autoubiquitinated by a novel mechanism wherein the catalytic cysteine, instead of a lysine residue, provides the polyubiquitin chain acceptor site, and this cysteine-linked chain functions as a degradation signal. The polyubiquitin chain can also be transferred to a lysine side chain, suggesting a mechanism for polyubiquitin chain assembly that precedes substrate modification.},
	keywords = {Amino Acids, Catalytic Domain, Cysteine, Fungal Proteins, Gene Expression Regulation, Fungal, Green Fluorescent Proteins, Microscopy, Fluorescence, Plasmids, Polyubiquitin, Proteasome Endopeptidase Complex, Protein Binding, ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Yeasts},
	author = {Ravid, Tommer and Hochstrasser, Mark}
}
