ArticleMolecular biology of the cell1997
Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
61 citing papers in PubMed, 163 citations in OpenAlex.
- Palmitic acid and palmitoylation in cancer: Understanding, insights, and challenges.Innovation (Cambridge (Mass.)) · 2025Review
- Context-dependent roles of palmitoylation in acute respiratory distress syndrome: integrating inflammation, cell death and repair.European respiratory review : an official journal of the European Respiratory Society · 2025Review
- D6PK plasma membrane polarity requires a repeated CXX(X)P motif and PDK1-dependent phosphorylation.Nature plants · 2024Article
- Ca2+-dependent protein acyltransferase DHHC21 controls activation of CD4+ T cells.Journal of cell science · 2022Article
- Review
- ProteinOpen biology · 2021Review
- Function of Protein S-Palmitoylation in Immunity and Immune-Related Diseases.Frontiers in immunology · 2021Review
- Article
- Regulation of T cell receptor signaling by protein acyltransferase DHHC21.Molecular biology reports · 2020Article
- Live-cell monitoring of protein localization to membrane rafts using protein-fragment complementation.Bioscience reports · 2020Article
- Protein Palmitoylation in Leukocyte Signaling and Function.Frontiers in cell and developmental biology · 2020Review
- Protein palmitoylation and cancer.EMBO reports · 2018Review
- Intrinsic properties and plasma membrane trafficking route of Src family kinase SH4 domains sensitive to retargeting by HIV-1 Nef.The Journal of biological chemistry · 2018Article
- Synapsins regulate brain-derived neurotrophic factor-mediated synaptic potentiation and axon elongation by acting on membrane rafts.The European journal of neuroscience · 2017Article
- Click-Chemistry Based High Throughput Screening Platform for Modulators of Ras Palmitoylation.Scientific reports · 2017Article
- Myristoylation: An Important Protein Modification in the Immune Response.Frontiers in immunology · 2017Review
- Progress toward Understanding Protein S-acylation: Prospective in Plants.Frontiers in plant science · 2017Review
- Identification of a family of fatty-acid-speciated sonic hedgehog proteins, whose members display differential biological properties.Cell reports · 2015Article
- The Fyn-ADAP Axis: Cytotoxicity Versus Cytokine Production in Killer Cells.Frontiers in immunology · 2015Review
- Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Members of the Src family of protein tyrosine kinases are localized to subspecialized regions of the plasma membrane. Herein we show that the N-terminal SH4 region of the Src family member p59fyn (Fyn) is both necessary and sufficient for targeting of Fyn and heterologous proteins to the plasma membrane and detergent-insoluble subdomains. Attachment of the first 16 amino acids of Fyn to a normally cytosolic protein, beta-galactosidase, resulted in distinct plasma membrane localization of the chimeric protein. Mutation of the palmitoylation site (cysteine-3) within Fyn16-beta-galactosidase or wild-type Fyn abrogated plasma membrane localization, resulting in redistribution of the mutant proteins into intracellular membranes. Substitution of the SH4 motif within Fyn with heterologous sequences from other palmitoylated proteins (G alpha o and GAP43) revealed that the presence of palmitate is sufficient to direct plasma membrane localization independent of surrounding amino acid sequences and myristate. Palmitoylated Fyn chimeras were also enriched in the Triton X-100-resistant matrix, whereas nonpalmitoylated forms of these proteins were detected in the detergent-soluble fraction. The palmitate moiety on Fyn exhibited a half-life of 1.5-2 h. In contrast, the half-life of the polypeptide backbone was 8 h, indicating that palmitoylation is a reversible modification. These studies establish that the palmitoylated SH4 sequence of Fyn can be used to specifically target proteins to the plasma membrane in a reversible manner.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.