Cited by 521Protein Kinase Regulation and GTPase SignalingLipid Membrane Structure and BehaviorCellular transport and secretion

Trafficking and signaling by fatty-acylated and prenylated proteins

Resh, Marilyn D·2006·Nature Chemical Biology

Abstract

A wide variety of signaling proteins are modified by covalently linked fatty acids and/or prenyl groups. These hydrophobic moieties, which include myristate, palmitate, farnesyl and geranylgeranyl, are more than just fat: they provide distinct information that modulates the specificity and efficiency of signal transduction. Recent studies show that lipid modification influences the movement of a signaling protein within the cell and its final destination. Protein lipidation can also confer reversible association with membranes and other signaling proteins. These findings provide new insights into the biochemical and biophysical mechanisms that regulate membrane targeting, trafficking and signaling by lipid-modified proteins.

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Crossref · 10.1038/nchembio834

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  • Protein fatty acylation plays an essential role in cell signaling, membrane trafficking, protein-membrane interactions, and cellular localization.

    “Protein fatty acylation has been known to play an essential role in cell signaling, membrane trafficking, protein-membrane interactions, and cellular localization.33”

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Authors
Resh, M. D.
Affiliations
Memorial Sloan Kettering Cancer Center (US)
Corresponding author
Resh, Marilyn D
Venue
Nature Chemical Biology
Published
2006-10-18
Volume
2
Issue
11
Pages
584-590
ISSN
  • 1552-4450 (ISSN-L)
  • 1552-4469
OpenAlex
W1990524685
Cited by
521
References
98
Citations by year
2026: 17 · 2025: 6 · 2024: 13 · 2023: 10 · 2022: 21 · 2021: 21 · 2020: 19 · 2019: 18 · 2018: 23 · 2017: 27 · 2016: 29 · 2015: 32 · 2014: 38 · 2013: 34 · 2012: 29
FWCI
2.33
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Chemical Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Cancer Institute (CA 72309, R01CA072309)
  • National Institute of General Medical Sciences (R01GM057966, GM57966)
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 › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
protein lipidation, fatty acid acylation, prenylation, myristoylation, palmitoylation, signal transduction, membrane targeting, protein trafficking, lipid-modified proteins, protein-protein interaction
MeSH terms
Acylation, Animals, Fatty Acids, Humans, Models, Biological, Proteins, Signal Transduction, Protein Prenylation, Protein Transport

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