Trafficking and signaling by fatty-acylated and prenylated proteins
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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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”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [33]
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Meitzler, J. L., Gray, J. J., & Hendrickson, T. L. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.035 · Cited by 18 · see citing works
- Authors
- Resh, M. D.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Resh, Marilyn D
- ORCID
- 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
- Licence
- www.springer.com/tdm (tdm)
- 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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