K-Ras4B lipoprotein synthesis: biochemical characterization, functional properties, and dimer formation.

Protein Expression and Purification
Alexey Dementiev

Abstract

K-Ras4B, a small GTPase and a key oncogene, plays a central role in the early steps of signal transduction from activated receptor tyrosine kinases by recruiting its downstream effectors to the cell membrane. Specific posttranslational modifications of K-Ras4B, including the addition of C-terminal farnesyl and methyl groups, mediate its proper membrane localization and signaling activity. The mechanism and molecular determinants underlying this selective membrane localization and molecular interactions with its many regulators and downstream effectors are largely unknown. Preparative amounts of the posttranslationally processed K-Ras4B protein are necessary to carry out structural, functional, and cell biological studies of this important oncogene. In this work we describe a simple and efficient method for synthesis of milligram quantities of functionally active, fully processed K-Ras4B. Using this preparation, we observe K-Ras4B dimerization in vitro; this has not been observed previously and could be important for its activity, membrane anchoring, and translocation between different cellular membranes.

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Citations

Sep 16, 2014·Trends in Biochemical Sciences·Hugo LavoieFrank Sicheri
Oct 12, 2013·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Alexander WerkmüllerRoland Winter
Jun 24, 2014·Chemistry : a European Journal·Markus Ritzefeld
Apr 25, 2015·Nature Reviews. Molecular Cell Biology·Hugo Lavoie, Marc Therrien
May 24, 2016·Angewandte Chemie·Lei ZhaoYao-Wen Wu
Jul 12, 2017·Molecular and Cellular Biology·Maho TakahashiPhilip J S Stork
Dec 13, 2017·Cold Spring Harbor Perspectives in Medicine·Yong ZhouJohn F Hancock
Dec 4, 2019·Chemistry : a European Journal·Mari Takahara, Noriho Kamiya
Jul 23, 2016·Bioconjugate Chemistry·Tom Mejuch, Herbert Waldmann
Oct 10, 2021·Nature Structural & Molecular Biology·Venkatesh P MysoreDavid E Shaw

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