MRAS: A Close but Understudied Member of the RAS Family
Open accessAbstract
MRAS is the closest relative to the classical RAS oncoproteins and shares most regulatory and effector interactions. However, it also has unique functions, including its ability to function as a phosphatase regulatory subunit when in complex with SHOC2 and protein phosphatase 1 (PP1). This phosphatase complex regulates a crucial step in the activation cycle of RAF kinases and provides a key coordinate input required for efficient ERK pathway activation and transformation by RAS. MRAS mutations rarely occur in cancer but deregulated expression may play a role in tumorigenesis in some settings. Activating mutations in MRAS (as well as SHOC2 and PP1) do occur in the RASopathy Noonan syndrome, underscoring a key role for MRAS within the RAS-ERK pathway. MRAS also has unique roles in cell migration and differentiation and has properties consistent with a key role in the regulation of cell polarity. Further investigations should shed light on what remains a relatively understudied RAS family member.
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Aberrant MRAS activity in cancer is rare.
“While aberrant MRAS activity in cancer is rare37”
From Co-targeting SOS1 enhances the antitumor effects of KRASG12C inhibitors by addressing intrinsic and acquired resistance (2024) · cites this paper as [37]
SOS1 and RasGRP1 facilitate GTP-loading of MRAS, which together with SHOC2 and PP1C forms a phosphatase complex that contributes to increased activation of RAS-MAPK signaling through dephosphorylation of inhibitory sites on RAF kinases.
“SOS1 and RasGRP1 have been shown to facilitate the GTP-loading of MRAS37,38, which, together with SHOC2 and PP1C, forms a phosphatase complex that contributes to the increased activation of RAS-MAPK signaling through dephosphorylation of inhibitory sites on RAF kinases40.”
From Co-targeting SOS1 enhances the antitumor effects of KRASG12C inhibitors by addressing intrinsic and acquired resistance (2024) · cites this paper as [37]
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- Authors
- Young, L. C., & Rodriguez-Viciana, P.
- Affiliations
- University of California, San Francisco (US)
- ORCID
- Young, Lucy C.
- Venue
- Cold Spring Harbor Perspectives in Medicine
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2018-01-08
- Volume
- 8
- Issue
- 12
- Pages
- a033621
- ISSN
- 2157-1422 (ISSN-L)
- PMC
- PMC6280710
- OpenAlex
- W2784165555
- Cited by
- 53
- References
- 67
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 18 · 2023: 7 · 2022: 10 · 2021: 2 · 2020: 2 · 2019: 1 · 2018: 1
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Medicine (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- 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 › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- mineralocorticoid receptor antagonists, Ras family, Ras/ERK pathway, SHOC2, protein phosphatase 1, Noonan syndrome, RASopathies, cell polarity, cell migration, cell differentiation, carcinogenesis, oncogenic mutations
- MeSH terms
- Cell Differentiation, Cell Movement, Gene Expression Regulation, Humans, Noonan Syndrome, Signal Transduction, Cell Polarity, ras Proteins, MAP Kinase Signaling System, Intracellular Signaling Peptides and Proteins, Protein Phosphatase 1, Carcinogenesis
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