Ras ubiquitination: coupling spatial sorting and signal transmission.
H-Ras, N-Ras, and K-Ras proteins have distinct biological properties, despite ubiquitous expression and similar affinities for regulators and effectors. C-terminal hypervariable regions that distinguish H-Ras, N-Ras, and K-Ras proteins direct them to distinct membrane compartments, where they may encounter regulators and effectors at different local concentrations. Jura and coworkers now report that these membrane-targeting domains direct differential ubiquitination of Ras proteins and so provide a molecular mechanism to explain the sorting process and, perhaps, some of the dramatic differences in biological potency among H-Ras, N-Ras, and K-Ras proteins.
Rodriguez-Viciana
Pablo
P
University of California, San Francisco, Comprehensive Cancer Center, 2340 Sutter Street, San Francisco, California 94115, USA.
McCormick
Frank
F
D000818:Animals; D006801:Humans; D011485:Protein Binding; D015398:Signal Transduction; D025801:Ubiquitin / Q000378:metabolism*; D018631:ras Proteins / Q000235:genetics / Q000378:metabolism*
D025801:Ubiquitin; D018631:ras Proteins