RAS Proteins and Their Regulators in Human Disease

Simanshu, Dhirendra K.; Nissley, Dwight V.; McCormick, Frank

doi:10.1016/j.cell.2017.06.009

Cited by 1,943Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesCellular transport and secretion

RAS Proteins and Their Regulators in Human Disease

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Simanshu, Dhirendra K., Nissley, Dwight V., McCormick, Frank·2017·Cell

DOI 10.1016/j.cell.2017.06.009PMC PMC5555610

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Abstract

RAS proteins are binary switches, cycling between ON and OFF states during signal transduction. These switches are normally tightly controlled, but in RAS-related diseases, such as cancer, RASopathies, and many psychiatric disorders, mutations in the RAS genes or their regulators render RAS proteins persistently active. The structural basis of the switch and many of the pathways that RAS controls are well known, but the precise mechanisms by which RAS proteins function are less clear. All RAS biology occurs in membranes: a precise understanding of RAS' interaction with membranes is essential to understand RAS action and to intervene in RAS-driven diseases.

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Farnesylation at the position 185 cysteine residue results in KRAS anchoring at the plasma membrane, initiating the activation of KRAS and its downstream signaling.
“In particular, farnesylation at the position 185 cysteine residue results in KRAS anchoring at the plasma membrane, initiating the activation of KRAS and its downstream signaling42.”
From Mechanisms of KRAS inhibitor resistance in KRAS-mutant colorectal cancer harboring Her2 amplification and aberrant KRAS localization (2025) · cites this paper as [42]
The “RAS Proteins in the Membrane” section says farnesylation of a C-terminal cysteine facilitates membrane association, which is essential for downstream signaling. Our copy does not identify that cysteine as residue 185 or say that farnesylation itself activates KRAS; it also describes additional membrane-targeting and processing steps. Page numbers are unavailable in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Post-translational modification of KRAS plays an important role in KRAS-MAPK pathway activation.
“Post-translational modification of KRAS plays an important role in KRAS–MAPK pathway activation.”
From Mechanisms of KRAS inhibitor resistance in KRAS-mutant colorectal cancer harboring Her2 amplification and aberrant KRAS localization (2025) · cites this paper as [42]
KRAS is one of the most frequently mutated oncogenes in cancer, yet efforts to directly target KRAS have been mostly unsuccessful because initial analyses of KRAS proteins indicated that they lack a clear pocket to which small molecules can bind with high affinity.
“KRAS is one of the most frequently mutated oncogenes in cancer, yet efforts to directly target KRAS have been mostly unsuccessful because initial analyses of KRAS proteins indicated that they lack a clear pocket to which small molecules can bind with high affinity [1, 2].”
From Anti-tumor efficacy of a potent and selective non-covalent KRASG12D inhibitor (2022) · cites this paper as [2]
Distinct KRAS alleles exhibit substantial biochemical and functional heterogeneity.
“Although KRAS mutations are often collectively classified as a single oncogenic entity, distinct KRAS alleles exhibit substantial biochemical and functional heterogeneity [1,4,12].”
From Precision Targeting of KRAS-Mutant Cancers: Beyond G12C Toward G12D and Pan-RAS Therapeutic Strategies (2026) · cites this paper as [4]
Mutational activation of KRAS promotes the initiation and progression of cancers, especially in the colorectum, pancreas, lung, and blood plasma, with varying prevalence of specific activating missense mutations.
“Mutational activation of KRAS promotes the initiation and progression of cancers, especially in the colorectum, pancreas, lung, and blood plasma, with varying prevalence of specific activating missense mutations.”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]

KRAS is frequently mutated in only a handful of cancers, with the highest frequencies in colorectal adenocarcinoma (COAD), lung adenocarcinoma (LUAD), multiple myeloma (MM), and pancreatic adenocarcinoma (PAAD).
“However, it is frequently mutated in only a handful of cancers, with the highest frequencies in colorectal adenocarcinoma (COAD), lung adenocarcinoma (LUAD), multiple myeloma (MM), and pancreatic adenocarcinoma (PAAD).”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
KRAS is one of the most commonly mutated genes in cancer.
“KRAS is one of the most commonly mutated genes in cancer1,2”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
When mutated at hotspot codons 12, 13, 61, or 146, activated KRAS protein hyperactivates many downstream effector pathways, such as MAPK and PI3K-AKT.
“When mutated at one of its four hotspot codons—12, 13, 61, or 146—activated KRAS protein hyperactivates many downstream effector pathways, such as the MAPK and PI3K-AKT signaling pathways1”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
SHP2 is involved in regulation of multiple signaling pathways, including RAS-MAPK, PI3K-AKT and JAK-STAT.
“As protein tyrosine phosphorylation plays an essential role in multiple intracellular processes, SHP2 is involved in the regulation of multiple signaling pathways, including those involved in cancer cells, such as RAS-MAPK, PI3K-AKT and JAK-STAT pathways.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [261]
RAS acts as a molecular switch, transmitting signals of cell growth and differentiation by binding to GTP or GDP and switching between active and inactive states.
“RAS acts as a molecular switch, transmitting signals of cell growth and differentiation by binding to GTP or GDP and switching between active and inactive states.261”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [261]
RAS pathway abnormalities, including activating RAS mutations, are common across many cancer types.
“abnormalities in components of the RAS pathway, including activating RAS mutations, are common across a diverse range of malignancies”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
KRAS, NRAS and HRAS cycle between GTP-bound on and GDP-bound off states through RAS-GEFs and RAS-GAPs.
“The RAS family GTPases, KRAS, NRAS and HRAS, cycle between GTP-loaded ‘on’ and GDP-loaded ‘off’ states4,6, involving the action of RAS-guanine nucleotide exchange factors (RAS-GEFs) and RAS-GTPase-activating proteins (RAS-GAPs), respectively.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
Almost all cancer-associated RAS mutations, about 95%, affect codon 12, 13 or 61 and cause a markedly increased basal RAS-GTP:RAS-GDP ratio and constitutive RAS effector activation.
“Almost all cancer-associated RAS mutations (~95%) affect codon 12, 13 or 61, and lead to a markedly increased basal RAS-GTP:RAS-GDP ratio and constitutive activation of RAS effectors4,6.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
Mutated RAS remains predominantly in the active GTP-bound state because GTP hydrolysis by its GTPase domain and by GTPase-activating proteins is impaired.
“When mutated, oncogenic RAS remains preferentially in the active GTP-bound state, whereas GTP hydrolysis by its GTPase function and enzymes such as GTPase-activating proteins, is compromised1,2.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [1]
KRAS is one of the most frequently mutated oncogenes in cancer and is commonly linked to therapeutic resistance and poor prognosis.
“KRAS in particular, is among the most frequently mutated oncogenes in cancer and is commonly associated with therapeutic resistance and poor prognosis1,5,6.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [1]
These mutations shift Ras equilibrium to the GTP-bound state and uncouple Ras from upstream receptor inputs, driving constitutive signaling to downstream effectors.
“These mutations dramatically shift the equilibrium of Ras protein to exist mostly in the GTP-bound state and effectively uncouple Ras proteins from upstream receptor inputs and drive constitutive signaling to downstream Ras effector pathways (13).”
From KRAS mutation in pancreatic cancer (2021) · cites this paper as [13]
The affinity of KRAS and GTP is at the pM level, while the concentration of GTP in cells is up to 0.5 μM.
“On the one hand, the affinity of KRAS and GTP is at the pM level, while the concentration of GTP in cells is up to 0.5 μM.”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [18]
It is difficult to achieve effective competition like protein kinase inhibitors.
“It is difficult to achieve effective competition like protein kinase inhibitors [18, 19].”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [18]
Oncogenic KRAS can activate various downstream effector pathways, and the best characterized are PI3K and MAPK.
“Oncogenic KRAS can activate various downstream effector pathways, and the best characterized are phosphatidylinositol 3-kinase (PI3K) and mitogen-activated protein kinases (MAPK) (23–25).”
From New Horizons in KRAS-Mutant Lung Cancer: Dawn After Darkness (2019) · cites this paper as [24]
The HVR and cell membrane have a substantial influence on KRAS dynamics and signaling.
“we recognize that these elements have a substantial influence on KRAS dynamics [53,54] and signaling [55].”
From Assessment of mutation probabilities of KRAS G12 missense mutants and their long-timescale dynamics by atomistic molecular simulations and Markov state modeling (2018) · cites this paper as [54]

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The Clinical KRAS(G12C) Inhibitor AMG 510 Drives Anti-Tumour Immunity
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EGFR Blockade Reverts Resistance to KRASG12C Inhibition in Colorectal Cancer.
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“Guanine exchange factors, such as SOS1, and GTPase activating proteins (GAP), such as NF1, directly mediate KRAS activation (2, 3).”
Background
Reactive Oxygen Species and Mitochondrial Dynamics: The Yin and Yang of Mitochondrial Dysfunction and Cancer Progression
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Suppression of the SLC7A11/glutathione axis causes synthetic lethality in KRAS-mutant lung adenocarcinoma
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KRAS mutation in pancreatic cancer
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FDA Approval Summary: Sotorasib for KRAS G12C -Mutated Metastatic NSCLC
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Single-Agent Divarasib (GDC-6036) in Solid Tumors with a KRAS G12C Mutation
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KRAS Dimerization Impacts MEK Inhibitor Sensitivity and Oncogenic Activity of Mutant KRAS
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Authors: Simanshu, D. K., Nissley, D. V., & McCormick, F.
Affiliations: Frederick National Laboratory for Cancer Research (US)
University of California, San Francisco (US)
Corresponding author: McCormick, Frank
ORCID: Simanshu, Dhirendra K.
Nissley, Dwight V.
McCormick, Frank
Venue: Cell
Publisher: Elsevier BV
Published: 2017-06
Volume: 170
Issue: 1
Pages: 17-33
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2017.06.009
PMC: PMC5555610
OpenAlex: W2732767128
Cited by: 1,943
References: 162
Citations by year: 2026: 210 · 2025: 263 · 2024: 276 · 2023: 247 · 2022: 267 · 2021: 247 · 2020: 194 · 2019: 143 · 2018: 82 · 2017: 12
FWCI: 11.03
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 393 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Cancer Institute
NIH (HHSN261200800001E)
Outstanding Investigator Award (5R35CA197709)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: Ras proteins, Ras signaling, RASopathies, cancer, mental illness, RAS mutations, signal transduction, membrane binding, Ras activation
MeSH terms: Congenital Abnormalities, Animals, Mental Disorders, Cell Membrane, Humans, Mutation, Neoplasms, Phylogeny, Yeasts, Signal Transduction, ras Proteins

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RAS Proteins and Their Regulators in Human Disease

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