Ronald P. Trible
National Institutes of Health
8 Papers
8 Citations
Ronald P. Trible is an academic researcher from National Institutes of Health. The author has contributed to research in topics: T-cell receptor & Linker for Activation of T cells. The author has an hindex of 7, co-authored 7 publications.
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Papers
LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation.
TL;DR: The cloning of the cDNA is reported for a highly tyrosine-phosphorylated 36-38 kDa protein, previously characterized by its association with Grb2, phospholipase C-gamma1, and the p85 subunit of phosphoinositide 3-kinase, which is phosphorylated by ZAP-70/Syk protein tyrosines leading to recruitment of multiple signaling molecules.
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LAT Palmitoylation: Its Essential Role in Membrane Microdomain Targeting and Tyrosine Phosphorylation during T Cell Activation
TL;DR: It is demonstrated that human LAT is palmitoylated and that palMIToylated LAT predominantly localizes into glycolipid-enriched microdomains (GEMs).
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Essential Role of LAT in T Cell Development
Weiguo Zhang,Connie L. Sommers,Deborah N. Burshtyn,Christopher C. Stebbins,Jan B. DeJarnette,Ronald P. Trible,Alexander Grinberg,Henry C. Tsay,Helena M. Jacobs,Craig M. Kessler,Eric O. Long,Paul E. Love,Lawrence E. Samelson +12 more
TL;DR: To probe the role of LAT in T cell development, the LAT gene was disrupted by targeting and normal B cell populations but the absence of any mature peripheral T cells were revealed.
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Association of Grb2, Gads, and Phospholipase C-γ1 with Phosphorylated LAT Tyrosine Residues EFFECT OF LAT TYROSINE MUTATIONS ON T CELL ANTIGEN RECEPTOR-MEDIATED SIGNALING
Weiguo Zhang,Weiguo Zhang,Ronald P. Trible,Minghua Zhu,Stanley K. Liu,C. Jane McGlade,Lawrence E. Samelson +6 more
TL;DR: The results strongly suggest that PLC-gamma activation regulates Ras activation in these cells, and show that three distal tyrosines, Tyr(171), Tyr(191), and Tyr(226), are responsible for Grb2-binding; Tyr( 171, and Tyr (191), but not Tyr( 226), are necessary for Gads binding.
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Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line
TL;DR: It is demonstrated that LAT is required for TCR-mediated Ca2+ mobilization and optimal tyrosine phosphorylation of phospholipase C-gamma1, Vav and SLP-76, and the use of a LAT-deficient cell line for the analysis of LAT structure and function is demonstrated.
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