Targeting protein prenylation for cancer therapy

Berndt, Norbert; Hamilton, Andrew D.; Sebti, Saïd M.

doi:10.1038/nrc3151

Cited by 622Protein Kinase Regulation and GTPase SignalingCancer, Lipids, and MetabolismProtein Tyrosine Phosphatases

Targeting protein prenylation for cancer therapy

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Berndt, Norbert, Hamilton, Andrew D., Sebti, Saïd M.·2011·Nature Reviews Cancer

DOI 10.1038/nrc3151PMC PMC4037130

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Abstract

Protein farnesylation and geranylgeranylation, together referred to as prenylation, are lipid post-translational modifications that are required for the transforming activity of many oncogenic proteins, including some RAS family members. This observation prompted the development of inhibitors of farnesyltransferase (FT) and geranylgeranyl-transferase 1 (GGT1) as potential anticancer drugs. In this Review, we discuss the mechanisms by which FT and GGT1 inhibitors (FTIs and GGTIs, respectively) affect signal transduction pathways, cell cycle progression, proliferation and cell survival. In contrast to their preclinical efficacy, only a small subset of patients responds to FTIs. Identifying tumours that depend on farnesylation for survival remains a challenge, and strategies to overcome this are discussed. One GGTI has recently entered the clinic, and the safety and efficacy of GGTIs await results from clinical trials.

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Farnesyltransferase inhibitors yielded preclinical responses but limited responses in clinical trials.
“This modification was the target of an active pipeline of farnesyltransferase inhibitors and yielded preclinical responses however limited responses in clinical trials12.”
From Selective KRAS G12C inhibitors in non-small cell lung cancer: chemistry, concurrent pathway alterations, and clinical outcomes (2021) · cites this paper as [12]

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Authors: Berndt, N., Hamilton, A. D., & Sebti, S. M.
Affiliations: Moffitt Cancer Center (US)
University of Oxford (GB)
ORCID: Hamilton, Andrew D.
Venue: Nature Reviews Cancer
Publisher: Springer Science and Business Media LLC
Published: 2011-10-24
Volume: 11
Issue: 11
Pages: 775-791
ISSN: 1474-175X (ISSN-L)
1474-1768
DOI: 10.1038/nrc3151
PMC: PMC4037130
OpenAlex: W2002252224
Cited by: 614
References: 221
Citations by year: 2026: 25 · 2025: 24 · 2024: 20 · 2023: 42 · 2022: 34 · 2021: 52 · 2020: 59 · 2019: 46 · 2018: 42 · 2017: 46 · 2016: 52 · 2015: 47 · 2014: 48 · 2013: 44 · 2012: 30
FWCI: 3.60
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature reviews. Cancer (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Cancer Institute (CA098473, U19CA067771, CA067771, R01CA098473)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: protein prenylation, farnesylation, geranylgeranylation, farnesyltransferase inhibitors, signal transduction, cell cycle progression, tumor cell survival, anticancer drug development, clinical trial results
MeSH terms: Ras Homolog Enriched in Brain Protein, Animals, Antineoplastic Agents, Cell Cycle, Cell Survival, Enzyme Inhibitors, Humans, Neoplasms, Neuropeptides, Signal Transduction, Randomized Controlled Trials as Topic, Protein Prenylation, Alkyl and Aryl Transferases, Monomeric GTP-Binding Proteins, Cell Proliferation, Farnesyltranstransferase, Molecular Targeted Therapy

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