Evidence map›Paper›PMID 38880243›Full record

ArticleMolecular & cellular proteomics : MCP2024

Profiling Proteins and Phosphorylation Sites During T Cell Activation Using an Integrated Thermal Shift Assay.

Brandon M Gassaway, Edward L Huttlin, Emily M Huntsman, Tomer M Yaron-Barir, Jared L Johnson, Kiran Kurmi, Lewis C Cantley, Joao A Paulo, Alison E Ringel, Steven P Gygi and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Brandon M GassawayDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA; Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah, USA.
Edward L HuttlinDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
Emily M HuntsmanMeyer Cancer Center and Department of Medicine, Weill Cornell Medicine, New York, New York, USA.
Tomer M Yaron-BarirMeyer Cancer Center and Department of Medicine, Weill Cornell Medicine, New York, New York, USA; Columbia University Vagelos College of Physicians and Surgeons, New York, New York, USA.
Jared L JohnsonDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA; Dana Farber Cancer Institute, Boston, Massachusetts, USA.
Kiran KurmiDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
Lewis C CantleyDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA; Dana Farber Cancer Institute, Boston, Massachusetts, USA.
Joao A PauloDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
Alison E RingelDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA; Ragon Institute of Mass General, MIT, and Harvard, Cambridge, Massachusetts, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA; Koch Institute for Integrative Cancer Research, Cambridge, Massachusetts, USA. Electronic address: aringel@mit.edu.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA. Electronic address: steven_gygi@hms.harvard.edu.
Marcia C HaigisDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA. Electronic address: marcia_haigis@hms.harvard.edu.

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI STEVEN P GYGI · 2003 to 2023
$2.0M
Defining mechanisms to promote antitumor immunity by modulating one-carbon metabolismR01CA276866 · NCI · HARVARD MEDICAL SCHOOL · 2024 to 2025
$1.1M
Role of Phosphoinositides and Protein Kinases in the control of Cancer MetabolismR35CA197588 · DANA-FARBER CANCER INST · 2025 to 2025
$1.1M
NCI NIH HHS K22 CA266150NCI NIH HHS R01 CA276866NCI NIH HHS R35 CA197588NIGMS NIH HHS R01 GM067945NIGMS NIH HHS R01 GM132129
6 · The paper itself

Abstract

T cell activation is a complex biological process of naive cells maturing into effector cells. Proteomic and phospho-proteomic approaches have provided critical insights into this process, yet it is not always clear how changes in individual proteins or phosphorylation sites have functional significance. Here, we developed the Phosphorylation Integrated Thermal Shift Assay (PITSA) that combines the measurement of protein or phosphorylation site abundance and thermal stability into a single tandem mass tags experiment and apply this method to study T cell activation. We quantified the abundance and thermal stability of over 7500 proteins and 5000 phosphorylation sites and identified significant differences in chromatin-related, TCR signaling, DNA repair, and proliferative phosphoproteins. PITSA may be applied to a wide range of biological contexts to generate hypotheses as to which proteins or phosphorylation sites are functionally regulated in a given system as well as the mechanisms by which this regulation may occur.

Indexed as

Lymphocyte ActivationProteomicsT-LymphocytesAnimalsHumansMicePhosphoproteinsPhosphorylationProtein StabilitySignal TransductionTandem Mass SpectrometryPhosphoproteinsCD8((+)) T cell activationcyclin-dependent kinase signalingDNA repairphosphoproteomicsproteome thermal stabilityproteomics

Identifiers

PMID38880243
PMCPMC11298636

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.