ArticleThe Journal of cell biology1999
Dual fatty acylation of p59(Fyn) is required for association with the T cell receptor zeta chain through phosphotyrosine-Src homology domain-2 interactions.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 106 citations in OpenAlex.
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- Recruitment, regulation, and release: Control of signaling enzyme localization and function by reversible S-acylation.The Journal of biological chemistry · 2024Review
- Dual Role of ACBD6 in the Acylation Remodeling of Lipids and Proteins.Biomolecules · 2022Article
- Effects of Electrical Stimulation on the Signal Transduction-Related Proteins, c-Src and Focal Adhesion Kinase, in Fibroblasts.Life (Basel, Switzerland) · 2022Article
- Ca2+-dependent protein acyltransferase DHHC21 controls activation of CD4+ T cells.Journal of cell science · 2022Article
- Insights into the post-translational modification and its emerging role in shaping the tumor microenvironment.Signal transduction and targeted therapy · 2021Review
- Regulation of Fibroblast Cell Polarity by Src Tyrosine Kinase.Biomedicines · 2021Article
- Function of Protein S-Palmitoylation in Immunity and Immune-Related Diseases.Frontiers in immunology · 2021Review
- Targeting cellular fatty acid synthesis limits T helper and innate lymphoid cell function during intestinal inflammation and infection.Mucosal immunology · 2021Article
- Article
- Sensitive FRET Biosensor Reveals Fyn Kinase Regulation by Submembrane Localization.ACS sensors · 2019Article
- mTORC1 Signaling Is Palmitoylation-Dependent in Hippocampal Neurons and Non-neuronal Cells and Involves Dynamic Palmitoylation of LAMTOR1 and mTOR.Frontiers in cellular neuroscience · 2019Article
- Myristoylation: An Important Protein Modification in the Immune Response.Frontiers in immunology · 2017Review
- IL-12 Signals through the TCR To Support CD8 Innate Immune Responses.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Tris DBA palladium is highly effective against growth and metastasis of pancreatic cancer in an orthotopic model.Oncotarget · 2016Article
- Site-specific functionalization of proteins and their applications to therapeutic antibodies.Computational and structural biotechnology journal · 2014Review
- Differential polarization of C-terminal Src kinase between naive and antigen-experienced CD8+ T cells.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Initiation of TCR phosphorylation and signal transduction.Frontiers in immunology · 2011Article
- Myristoylation and membrane binding regulate c-Src stability and kinase activity.Molecular and cellular biology · 2010Article
- N-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2010Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The first 10 residues within the Src homology domain (SH)-4 domain of the Src family kinase Fyn are required for binding to the immune receptor tyrosine-based activation motif (ITAM) of T cell receptor (TCR) subunits. Recently, mutation of glycine 2, cysteine 3, and lysines 7 and 9 was shown to block binding of Fyn to TCR zeta chain ITAMs, prompting the designation of these residues as an ITAM recognition motif (Gauen, L.K.T., M.E. Linder, and A.S. Shaw. 1996. J. Cell Biol. 133:1007-1015). Here we show that these residues do not mediate direct interactions with TCR ITAMs, but rather are required for efficient myristoylation and palmitoylation of Fyn. Specifically, coexpression of a K7,9A-Fyn mutant with N-myristoyltransferase restored myristoylation, membrane binding, and association with the cytoplasmic tail of TCR zeta fused to CD8. Conversely, treatment of cells with 2-hydroxymyristate, a myristoylation inhibitor, blocked association of wild-type Fyn with zeta. The Fyn NH2 terminus was necessary but not sufficient for interaction with zeta and both Fyn kinase and SH2 domains were required, directing phosphorylation of zeta ITAM tyrosines and binding to zeta ITAM phosphotyrosines. Fyn/zeta interaction was sensitive to octylglucoside and filipin, agents that disrupt membrane rafts. Moreover, a plasma membrane bound, farnesylated Fyn construct, G2A,C3S-FynKRas, was not enriched in the detergent insoluble fraction and did not associate with zeta. We conclude that the Fyn SH4 domain provides the signals for fatty acylation and specific plasma membrane localization, stabilizing the interactions between the Fyn SH2 domain and phosphotyrosines in TCR zeta chain ITAMs.
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