Evidence map›Paper›PMID 25278942›Full record

ReviewFrontiers in immunology2014

Regulation of fc receptor endocytic trafficking by ubiquitination.

Rosa Molfetta, Linda Quatrini, Francesca Gasparrini, Beatrice Zitti, Angela Santoni, Rossella Paolini

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2014. 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
3.2field-weighted citation impact, top 9% 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, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. In Translation: FcRn across the Therapeutic Spectrum.International journal of molecular sciences · 2021
    Review
  10. Human Platelets Take up Anti-VEGF Agents.Journal of ophthalmology · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
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  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

6 authors at 2 institutions in 2 countries.

Rosa MolfettaDepartment of Molecular Medicine, "Sapienza" University of Rome , Rome , Italy.
Linda QuatriniDepartment of Molecular Medicine, "Sapienza" University of Rome , Rome , Italy.
Francesca GasparriniLymphocyte Interaction Laboratory, London Research Institute, Cancer Research UK , London , UK.
Beatrice ZittiDepartment of Molecular Medicine, "Sapienza" University of Rome , Rome , Italy.
Angela SantoniDepartment of Molecular Medicine, "Sapienza" University of Rome , Rome , Italy ; Institute Pasteur-Fondazione Cenci Bolognetti, "Sapienza" University of Rome , Rome , Italy.
Rossella PaoliniDepartment of Molecular Medicine, "Sapienza" University of Rome , Rome , Italy ; Institute Pasteur-Fondazione Cenci Bolognetti, "Sapienza" University of Rome , Rome , Italy.
Sapienza University of Rome · ITCancer Research UK · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most immune cells, particularly phagocytes, express various receptors for the Fc portion of the different immunoglobulin isotypes (Fc receptors, FcRs). By binding to the antibody, they provide a link between the adaptive immune system and the powerful effector functions triggered by innate immune cells such as mast cells, neutrophils, macrophages, and NK cells. Upon ligation of the immune complexes, the downstream signaling pathways initiated by the different receptors are quite similar for different FcR classes leading to the secretion of preformed and de novo synthesized pro-inflammatory mediators. FcR engagement also promotes negative signals through the combined action of several molecules that limit the extent and duration of positive signaling. To this regard, ligand-induced ubiquitination of FcRs for IgE (FcεR) and IgG (FcγR) has become recognized as a key modification that generates signals for the internalization and/or delivery of engaged receptor complexes to lysosomes or cytoplasmic proteasomes for degradation, providing negative-feedback regulation of Fc receptor activity. In this review, we discuss recent advances in our understanding of the molecular mechanisms that ensure the clearance of engaged Fcε and Fcγ receptor complexes from the cell surface with an emphasis given to the cooperation between the ubiquitin pathway and endosomal adaptors including the endosomal sorting complex required for transport (ESCRT) in controlling receptor internalization and sorting along the endocytic compartments.

Indexed as

endocytic adaptorsendocytosisFc receptorsinnate immune cellsubiquitination

Identifiers

PMID25278942
PMCPMC4166898
OpenAlexW2069814690

What OpenQuestion 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 OpenQuestion graph.