Cited by 1,467Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesCellular transport and secretion

Ras oncogenes: split personalities

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Karnoub, Antoine E., Weinberg, Robert A.·2008·Nature Reviews Molecular Cell Biology

Abstract

Extensive research on the Ras proteins and their functions in cell physiology over the past 30 years has led to numerous insights that have revealed the involvement of Ras not only in tumorigenesis but also in many developmental disorders. Despite great strides in our understanding of the molecular and cellular mechanisms of action of the Ras proteins, the expanding roster of their downstream effectors and the complexity of the signalling cascades that they regulate indicate that much remains to be learnt.

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Crossref · 10.1038/nrm2438

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  • PDEδ has a large hydrophobic pocket that can bind farnesyl proteins, especially the lipid portion of KRAS protein, thereby preventing the farnesyl modification of KRAS protein from binding to cell membrane and inhibiting tumor cell proliferation and growth.

    “PDEδ has a large hydrophobic pocket that can bind farnesyl proteins, especially the lipid portion of KRAS protein, thereby preventing the farnesyl modification of KRAS protein from binding to cell membrane and inhibiting tumor cell proliferation and growth.339,340”

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Authors
Karnoub, A. E., & Weinberg, R. A.
Affiliations
Whitehead Institute for Biomedical Research (US)
Venue
Nature Reviews Molecular Cell Biology
Published
2008-07
Volume
9
Issue
7
Pages
517-531
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
OpenAlex
W2004774286
Cited by
1,467
References
234
Citations by year
2026: 28 · 2025: 48 · 2024: 58 · 2023: 60 · 2022: 67 · 2021: 89 · 2020: 74 · 2019: 87 · 2018: 93 · 2017: 95 · 2016: 103 · 2015: 118 · 2014: 100 · 2013: 108 · 2012: 94
FWCI
6.15
Type
journal article
Language
en
Open access
Locations
  • Nature Reviews Molecular Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Cancer Institute (P01 CA08111, U54 CA12515, P01CA080111, P50CA089393)
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
oncogenic Ras, carcinogenesis, developmental disorders, downstream effectors, cell physiology, Ras proteins
MeSH terms
Amino Acid Sequence, Animals, Cell Transformation, Neoplastic, DNA-Binding Proteins, Enzyme Activation, Gene Expression Regulation, Humans, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Processing, Post-Translational, Genes, ras, Transcription Factors, Signal Transduction, Sequence Alignment, ras Proteins, Phosphatidylinositol 3-Kinases, GTPase-Activating Proteins, Mitogen-Activated Protein Kinases

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