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Autopromotion of K-Ras4B Feedback Activation Through an SOS-Mediated Long-Range Allosteric Effect

Xuan He, Kui Du, Yuanhao Wang, Jigang Fan, Mingyu Li, Duan Ni, Shaoyong Lu, Xiaolan Bian, Yaqin Liu

2022Frontiers in Molecular Biosciences13 citationsDOIOpen Access PDF

Abstract

The Ras-specific guanine nucleotide exchange factors Son of Sevenless (SOS) regulates Ras activation by converting inactive GDP-bound to active GTP-bound states. The catalytic activity of Ras is further allosterically regulated by GTP−Ras bound to a distal site through a positive feedback loop. To address the mechanism underlying the long-range allosteric activation of the catalytic K-Ras4B by an additional allosteric GTP–Ras through SOS, we employed molecular dynamics simulation of the K-Ras4B G13D •SOS cat complex with and without an allosteric GTP-bound K-Ras4B G13D . We found that the binding of an allosteric GTP−K-Ras4B G13D enhanced the affinity between the catalytic K-Ras4B G13D and SOS cat , forming a more stable conformational state. The peeling away of the switch I from the nucleotide binding site facilitated the dissociation of GDP, thereby contributing to the increased nucleotide exchange rate. The community networks further showed stronger edge connection upon allosteric GTP−K-Ras4B G13D binding, which represented an increased interaction between catalytic K-Ras4B G13D and SOS cat . Moreover, GTP−K-Ras4B G13D binding transmitted allosteric signaling pathways though the Cdc25 domain of SOS that enhanced the allosteric regulatory from the K-Ras4B G13D allosteric site to the catalytic site. This study may provide an in-depth mechanism for abnormal activation and allosteric regulation of K-Ras4B G13D .

Topics & Concepts

Allosteric regulationRange (aeronautics)ChemistryBiophysicsBiologyBiochemistryMaterials scienceEnzymeComposite materialProtein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysReceptor Mechanisms and Signaling