1. Brother’s Keeper: Wild-Type Mutant K-Ras Dimers Limit Oncogenesis
Yi-Jang Lin, Kevin M. Haigis 
Cell 
Volume 172, Issue 4, Pages (February 2018)
DOI: /j.cell
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2. Figure 1 Alternative Models for K-Ras Signaling
(A) In the dimer model, the salt bridge formed between D154 of one K-Ras molecule and R161 of a partner molecule allows for dimerization. A heterodimer between WT and mutant K-Ras would create a dimer than cannot promote the Raf-1/B-Raf heterodimer required for MAPK signaling. A homodimer between two molecules of mutant K-Ras would create a dimer than can promote MAPK signaling. The D154Q mutant would disrupt both of these dimers.
(B) In this non-dimer model, D154 is required for interaction with effectors. WT (GDP-bound) K-Ras provides an anti-proliferative signal that is lost in the D154Q mutant. Moreover, K-Ras dimerization could be the by-product of effector dimerization, and D154Q would appear to disrupt dimer formation because it prevents association with the effectors (like Raf proteins) that provide the dimerization interface.
Cell  , DOI: ( /j.cell )
Copyright © 2018 Elsevier Inc. Terms and Conditions