Ras ubiquitination: coupling spatial sorting and signal transmission

Cancer Cell
Pablo Rodriguez-Viciana, Frank McCormick

Abstract

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.

References

Oct 23, 2003·Annual Review of Cell and Developmental Biology·Linda Hicke, Rebecca Dunn
Jul 21, 2004·Current Opinion in Cell Biology·Marta MiaczynskaMarino Zerial
Feb 12, 2005·Science·Oliver RocksPhilippe I H Bastiaens
Oct 18, 2005·Nature Reviews. Molecular Cell Biology·Walter Kolch

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Citations

Feb 23, 2007·Cell Structure and Function·Takashi FukanoAtsushi Miyawaki
Dec 10, 2016·PloS One·Hossein NakhaeizadehMohammad Reza Ahmadian
Feb 20, 2018·Critical Reviews in Biochemistry and Molecular Biology·Saeideh Nakhaei-RadMohammad Reza Ahmadian

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