Protein regulation by monoubiquitin.
Multi-ubiquitin chains at least four subunits long are required for efficient recognition and degradation of ubiquitylated proteins by the proteasome, but other functions of ubiquitin have been discovered that do not involve the proteasome. Some proteins are modified by a single ubiquitin or short ubiquitin chains. Instead of sending proteins to their death through the proteasome, monoubiquitylation regulates processes that range from membrane transport to transcriptional regulation.
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University Evanston, Illinois 60208, USA. l-hicke@northwestern.edu
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D000818:Animals; D001665:Binding Sites; D004705:Endocytosis; D006657:Histones / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D014452:Ubiquitins / Q000737:chemistry / Q000378:metabolism*
D006657:Histones; D011506:Proteins; D014452:Ubiquitins