Structural complexity in ubiquitin recognition.
Ubiquitinated proteins are sorted into distinct pathways via association with several classes of ubiquitin binding domain-containing proteins. A virtual explosion in the field of ubiquitin binding proteins has revealed several new classes and interactions with distinct surfaces on ubiquitin, providing a clearer understanding of how sorting of ubiquitinated proteins is achieved.
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. wade_harper@hms.harvard.edu
J Wade
JW
Harper
Brenda A
BA
Schulman
D000818:Animals; D020662:Guanine Nucleotide Exchange Factors / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary / Q000502:physiology; D021381:Protein Transport; D015398:Signal Transduction / Q000502:physiology*; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism*
D020662:Guanine Nucleotide Exchange Factors; C108382:RABGEF1 protein, human; D025801:Ubiquitin