Evidence map›Paper›PMID 23741050›Full record

ArticleMolecular biology of the cell2013

Multivalent immune complexes divert FcRn to lysosomes by exclusion from recycling sorting tubules.

Andrew W Weflen, Nina Baier, Qing-Juan Tang, Malon Van den Hof, Richard S Blumberg, Wayne I Lencer, Ramiro H Massol

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

67 citing papers in PubMed, 96 citations in OpenAlex.

  1. Trial
  2. Review
  3. Targeting FcRn for immunomodulation: a promising therapy in autoimmune inflammatory rheumatic diseases.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
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7 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

7 authors at 2 institutions in 3 countries.

Andrew W WeflenDivision of Gastroenterology, Boston Children's Hospital, Boston, MA 02115, USA.
Nina Baier
Qing-Juan Tang
Malon Van den Hof
Richard S Blumberg
Wayne I Lencer
Ramiro H Massol
Boston Children's Hospital · USBrigham and Women's Hospital · US

Funding

STRUCTURE-FUNCTION RELATIONSHIPS IN THE ALIMENTARY TRACTP30DK034854 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAYNE I LENCER · 1986 to 2026
$32.4M
INTESTINAL TRANSCYTOSIS OF IGG IN ADULT LIFER01DK053056 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI BLUMBERG, RICHARD S · 1997 to 2021
$10.6M
Endoplasmic reticulum stress and intestinal inflammationR01DK088199 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI Richard S Blumberg · 2010 to 2026
$9.6M
Training Program in Newborn and Developmental DiseasesT32HD007466 · NICHD · CHILDREN'S HOSPITAL BOSTON · PI KOUREMBANAS, STELLA · 1994 to 2016
$8.0M
Intestinal Disease-enterocyte toxin interactionR37DK048106 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI LENCER, WAYNE I · 2011 to 2020
$7.0M
FcRn-dependent sorting of IgG and IgG-opsinized antigens by epithelial cellsR01DK084424 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI LENCER, WAYNE I · 2009 to 2013
$1.9M
NICHD NIH HHS 5T32HD7466-14NICHD NIH HHS T32 HD007466NIDDK NIH HHS DK084424NIDDK NIH HHS DK53056NIDDK NIH HHS P30 DK034854NIDDK NIH HHS P30 DK34854NIDDK NIH HHS R01 DK053056NIDDK NIH HHS R01 DK084424NIDDK NIH HHS R01 DK088199NIDDK NIH HHS R37 DK048106
6 · The paper itself

Abstract

The neonatal receptor for immunoglobulin G (IgG; FcRn) prevents IgG degradation by efficiently sorting IgG into recycling endosomes and away from lysosomes. When bound to IgG-opsonized antigen complexes, however, FcRn traffics cargo into lysosomes, where antigen processing can occur. Here we address the mechanism of sorting when FcRn is bound to multivalent IgG-opsonized antigens. We find that only the unbound receptor or FcRn bound to monomeric IgG is sorted into recycling tubules emerging from early endosomes. Cross-linked FcRn is never visualized in tubules containing the unbound receptor. Similar results are found for transferrin receptor, suggesting a general mechanism of action. Deletion or replacement of the FcRn cytoplasmic tail does not prevent diversion of trafficking to lysosomes upon cross-linking. Thus physical properties of the lumenal ligand-receptor complex appear to act as key determinants for sorting between the recycling and lysosomal pathways by regulating FcRn entry into recycling tubules.

Indexed as

Animalsbeta 2-MicroglobulinCell LineCross-Linking ReagentsEndosomesGreen Fluorescent ProteinsHemagglutininsHistocompatibility Antigens Class IHumansImmunoglobulin GLysosomesMiceProtein BindingProtein Structure, TertiaryProtein TransportReceptors, Fcbeta 2-MicroglobulinCross-Linking Reagentsenhanced green fluorescent proteinFc receptor, neonatalGreen Fluorescent ProteinsHemagglutininsHistocompatibility Antigens Class IImmunoglobulin GReceptors, FcReceptors, Polymeric ImmunoglobulinReceptors, TransferrinRecombinant Fusion Proteins

Identifiers

PMID23741050
PMCPMC3727932
OpenAlexW2100906567

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.