Evidence map›Paper›PMID 24412752›Full record

ArticleCellular signalling2014

Activated PLC-γ1 is catalytically induced at LAT but activated PLC-γ1 is localized at both LAT- and TCR-containing complexes.

Noemi Cruz-Orcutt, Aldo Vacaflores, Sean F Connolly, Stephen C Bunnell, Jon C D Houtman

Abstract read
In one paragraph

Article in Cellular signalling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Noemi Cruz-OrcuttDepartment of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States.
Aldo VacafloresInterdisciplinary Graduate Program in Immunology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States.
Sean F ConnollyInterdisciplinary Graduate Program in Immunology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States.
Stephen C BunnellProgram in Immunology, Sackler School of Graduate Biomedical Sciences, Boston, MA 02111, United States; Department of Pathology, Tufts University School of Medicine, Boston, MA 02111, United States.
Jon C D HoutmanDepartment of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States; Interdisciplinary Graduate Program in Immunology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, United States. Electronic address: jon-houtman@uiowa.edu.
University of Iowa · USTufts University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN IMMUNOLOGYT32AI007485 · NIAID · UNIVERSITY OF IOWA · PI Kevin L Legge · 1995 to 2026
$5.4M
Cooperative SH2 and SH3 domain-mediated interactions at the adaptor protein Grb2R01CA136729 · NCI · UNIVERSITY OF IOWA · PI HOUTMAN, JON C.D. · 2010 to 2014
$1.6M
NCI NIH HHS R01 CA136729NIAID NIH HHS T32 AI007485
6 · The paper itself

Abstract

Phospholipase C-γ1 (PLC-γ1) is a key regulator of T cell receptor (TCR)-induced signaling. Activation of the TCR enhances PLC-γ1 enzymatic function, resulting in calcium influx and the activation of PKC family members and RasGRP. The current model is that phosphorylation of LAT tyrosine 132 facilitates the recruitment of PLC-γ1, leading to its activation and function at the LAT complex. In this study, we examined the phosphorylation kinetics of LAT and PLC-γ1 and the cellular localization of activated PLC-γ1. We observed that commencement of the phosphorylation of LAT tyrosine 132 and PLC-γ1 tyrosine 783 occurred simultaneously, supporting the current model. However, once begun, PLC-γ1 activation occurred more rapidly than LAT tyrosine 132. The association of LAT and PLC-γ1 was more transient than the interaction of LAT and Grb2 and a pool of activated PLC-γ1 translocated away from LAT to cellular structures containing the TCR. These studies demonstrate that LAT and PLC-γ1 form transient interactions that catalyze the activation of PLC-γ1, but that activated PLC-γ1 resides in both LAT and TCR clusters. Together, this work highlights that our current model is incomplete and the activation and function of PLC-γ1 in T cells is highly complex.

Indexed as

Adaptor Proteins, Signal TransducingGRB2 Adaptor ProteinHumansJurkat CellsKineticsMembrane ProteinsPhospholipase C gammaPhosphorylationProtein BindingReceptors, Antigen, T-CellSignal TransductionT-LymphocytesAdaptor Proteins, Signal TransducingGRB2 Adaptor ProteinLAT protein, humanMembrane ProteinsPhospholipase C gammaReceptors, Antigen, T-CellGrb2LATPhosphorylation kineticsPLC-γ1TCR

Identifiers

PMID24412752
PMCPMC3935424
OpenAlexW1976347910

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.