Evidence map›Paper›PMID 22577148›Full record

ArticleThe Journal of biological chemistry2012

Arginylated calreticulin at plasma membrane increases susceptibility of cells to apoptosis.

Cecilia López Sambrooks, Marcos A Carpio, Marta E Hallak

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Stress Granules: Novel Regulators of Programmed Cell Death.Mini reviews in medicinal chemistry · 2026
    Review
  4. Article
  5. Article
  6. tRNAmicroPublication biology · 2024
    Article
  7. Article
  8. Stress Granules in Cancer.Reviews of physiology, biochemistry and pharmacology · 2023
    Article
  9. Protein Arginylation: Milestones of Discovery.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Assaying the Posttranslational Arginylation of Proteins in Cultured Cells.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. Review
  12. Article
  13. tRNACell chemical biology · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Cecilia López SambrooksCentro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC-CONICET), Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, 5000 Cordoba, Argentina.
Marcos A Carpio
Marta E Hallak
Consejo Nacional de Investigaciones Científicas y Técnicas · ARResearch Centre in Biological Chemistry of Córdoba · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications of proteins are important for the regulation of cell fate and functions; one of these post-translational modifications is arginylation. We have previously established that calreticulin (CRT), an endoplasmic reticulum resident, is also one of the arginylated substrates found in the cytoplasm. In the present study, we describe that arginylated CRT (R-CRT) binds to the cell membrane and identified its role as a preapoptotic signal. We also show that cells lacking arginyl-tRNA protein transferase are less susceptible to apoptosis than wild type cells. Under these conditions R-CRT is present on the cell membrane but at early stages is differently localized in stress granules. Moreover, cells induced to undergo apoptosis by arsenite show increased R-CRT on their cell surface. Exogenously applied R-CRT binds to the cell membrane and is able to both increase the number of cells undergoing apoptosis in wild type cells and overcome apoptosis resistance in cells lacking arginyl-tRNA protein transferase that express R-CRT on the cell surface. Thus, these results demonstrate the importance of surface R-CRT in the apoptotic response of cells, implying that post-translational arginylation of CRT can regulate its intracellular localization, cell function, and survival.

Indexed as

ApoptosisAminoacyltransferasesAnimalsArginineBiotinylationCalciumCalreticulinCell MembraneEndoplasmic ReticulumFibroblastsFlow CytometryMiceMice, TransgenicProtein Processing, Post-TranslationalStreptavidinAminoacyltransferasesArgininearginyltransferaseCalciumCalreticulinStreptavidin

Identifiers

PMID22577148
PMCPMC3381163
OpenAlexW2094104236

What OpenQuestion holds

Textmetadata
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.