NDLI: Dual Fatty Acylation of p59 Fyn Is Required for Association with the T Cell Receptor ζ Chain through Phosphotyrosine

Content Provider	PubMed Central
Author	Hof, Woutervan't Resh, Marilyn D.
Copyright Year	1999
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 ζ 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 ζ fused to CD8. Conversely, treatment of cells with 2-hydroxymyristate, a myristoylation inhibitor, blocked association of wild-type Fyn with ζ. The Fyn NH2 terminus was necessary but not sufficient for interaction with ζ and both Fyn kinase and SH2 domains were required, directing phosphorylation of ζ ITAM tyrosines and binding to ζ ITAM phosphotyrosines. Fyn/ζ 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 ζ. 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 ζ chain ITAMs.
Starting Page	377
File Format	PDF
ISSN	15408140
e-ISSN	15408140
Journal	The Journal of Cell Biology
Issue Number	2
Volume Number	145
Language	English
Publisher	The Rockefeller University Press
Publisher Date	1999-04-19
Access Restriction	Open
Rights Holder	The Rockefeller University Press
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine

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Dual Fatty Acylation of p59Fyn Is Required for Association with the T Cell Receptor ζ Chain through Phosphotyrosine–Src Homology Domain-2 Interactions

Dual Fatty Acylation of p59Fyn Is Required for Association with the T Cell Receptor ζ Chain through Phosphotyrosine–Src Homology Domain-2 Interactions

Dual fatty acylation of p59(Fyn) is required for association with the T cell receptor zeta chain through phosphotyrosineSrc homology domain-2 interactions (1999)

Dual Fatty Acylation of $p59^{Fyn}$ Is Required for Association with the T Cell Receptor ζ Chain through Phosphotyrosine–Src Homology Domain-2 Interactions

Association of p59 fyn with the T Lymphocyte Costimulatory Receptor CD2 BINDING OF THE Fyn Src HOMOLOGY (SH) 3 DOMAIN IS REGULATED BY THE Fyn SH2 DOMAIN

Multiple features of the p59 ryn src homology 4 domain define a motif for immune-receptor tyrosine-based activation motif (itam) binding and for plasma membrane localization (1996).

Lipids Regulate Lck Protein Activity through Their Interactions with the Lck Src Homology 2 Domain

Lipids Regulate Lck Protein Activity through Their Interactions with the Lck Src Homology 2 Domain

Rapid T-cell receptor-mediated tyrosine phosphorylation of p120, an Fyn/Lck Src homology 3 domain-binding protein.

Dual Fatty Acylation of p59 Fyn Is Required for Association with the T Cell Receptor ζ Chain through Phosphotyrosine–Src Homology Domain-2 Interactions

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