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Cited by 838

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

LAT Palmitoylation

Open access
Zhang, Weiguo, Trible, Ronald P, Samelson, Lawrence E·1998·Immunity

Abstract

The linker molecule LAT is a critical substrate of the tyrosine kinases activated upon TCR engagement. Phosphorylated LAT binds Grb2, PLC-gamma1, and other signaling molecules. We demonstrate that human LAT is palmitoylated and that palmitoylated LAT predominantly localizes into glycolipid-enriched microdomains (GEMs). Although the LAT transmembrane domain is sufficient for membrane localization, palmitoylation at C26 and C29 is essential for efficient partitioning into GEMs. LAT palmitoylation is necessary for its tyrosine phosphorylation. After T cell activation, most tyrosine-phosphorylated LAT molecules and a fraction of PLC-gamma1 and other signaling molecules are present in GEMs. LAT is central to T cell activation and is a novel linker molecule shown to require targeting to membrane microdomains for signaling.

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Crossref · 10.1016/s1074-7613(00)80606-8

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Metadata

Authors
Zhang, W., Trible, R. P., & Samelson, L. E.
Venue
Immunity
Publisher
Elsevier BV
Published
1998-08
Volume
9
Issue
2
Pages
239-246
ISSN
1074-7613 (ISSN-L)
OpenAlex
W95054676
Cited by
838
References
3
FWCI
26.68
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: LAT Palmitoylation. https://app.cochat.ai/papers/10.1016/s1074-7613(00)80606-8
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Zhang, W., Trible, R. P., & Samelson, L. E. (1998). LAT Palmitoylation. Immunity. https://doi.org/10.1016/s1074-7613(00)80606-8

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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