Evidence map›Paper›PMID 34626566›Full record

ArticleMolecular cell2021

Proteome-wide mapping of short-lived proteins in human cells.

Jiaming Li, Zhenying Cai, Laura Pontano Vaites, Ning Shen, Dylan C Mitchell, Edward L Huttlin, Joao A Paulo, Brian L Harry, Steven P Gygi

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

95 citing papers in PubMed, 162 citations in OpenAlex.

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  9. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
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  20. Observational

35 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 1 country.

Jiaming LiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Zhenying CaiDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Laura Pontano VaitesDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Ning ShenDepartment of Biomedical Informatics, Harvard Medical School, Boston, MA 02115, USA.
Dylan C MitchellDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Edward L HuttlinDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Joao A PauloDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Brian L HarryDepartment of Pathology, Massachusetts General Hospital, Boston, MA 02114, USA; Department of Pathology, University of Colorado, Anschutz Medical Campus, Aurora, CO 80045, USA. Electronic address: brian.harry@cuanschutz.edu.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: steven_gygi@hms.harvard.edu.
Harvard University · USMassachusetts General Hospital · US

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
Advancing Multiplexed Isobaric Tag-based Strategies for Proteome ProfilingR01GM132129 · NIGMS · HARVARD MEDICAL SCHOOL · PI PAULO, JOAO A · 2019 to 2023
$1.7M
NIGMS NIH HHS R01 GM067945NIGMS NIH HHS R01 GM132129
6 · The paper itself

Abstract

Rapid protein degradation enables cells to quickly modulate protein abundance. Dysregulation of short-lived proteins plays essential roles in disease pathogenesis. A focused map of short-lived proteins remains understudied. Cycloheximide, a translational inhibitor, is widely used in targeted studies to measure degradation kinetics for short-lived proteins. Here, we combined cycloheximide chase assays with advanced quantitative proteomics to map short-lived proteins under translational inhibition in four human cell lines. Among 11,747 quantified proteins, we identified 1,017 short-lived proteins (half-lives ≤ 8 h). These short-lived proteins are less abundant, evolutionarily younger, and less thermally stable than other proteins. We quantified 103 proteins with different stabilities among cell lines. We showed that U2OS and HCT116 cells express truncated forms of ATRX and GMDS, respectively, which have lower stability than their full-length counterparts. This study provides a large-scale resource of human short-lived proteins under translational arrest, leading to untapped avenues of protein regulation for therapeutic interventions.

Indexed as

ProteomeAlanineCell LineCell Line, TumorCycloheximideFucoseGemininHCT116 CellsHEK293 CellsHumansPeptidesPrincipal Component AnalysisProtein BiosynthesisProteinsProteomicsQuality ControlAlanineazidohomoalanineCycloheximideFucoseGemininPeptidesProteinsProteomeRNA, Small Interferingmultiplexed quantitative proteomicsprotein degradationprotein half-livesshort-lived proteinsTMTpro tags

Identifiers

PMID34626566
PMCPMC8892350
OpenAlexW3204360192

What Socratic 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 Socratic graph.