Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dimerization of the polymeric immunoglobulin receptor controls its transcytotic trafficking.

Molecular biology of the cell - 1 Apr 1998

Singer K L, Mostov K E

Abstract excerpt

Binding of dimeric immunoglobulin (Ig)A to the polymeric Ig receptor (pIgR) stimulates transcytosis of pIgR across epithelial cells. Through the generation of a series of pIgR chimeric constructs, we have tested the ability of ligand to promote receptor dimerization and the subsequent role of receptor dimerization on its intracellular trafficking. Using the cytoplasmic domain of the T cell receptor-zeta chain as...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Biological Transport
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 9529387
DOI: 10.1091/mbc.9.4.901
PMCID: PMC25316

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dimerization of the polymeric immunoglobulin receptor controls its transcytotic trafficking.PMID 9529387Read ↗

Domain deletions in the human polymeric Ig receptor disclose differences between its dimeric IgA and pentameric IgM interaction.Semantic proximity Read ↗

Transcytosis of the polymeric Ig receptor requires phosphorylation of serine 664 in the absence but not the presence of dimeric IgA.Semantic proximity Read ↗

Transduction of basolateral-to-apical signals across epithelial cells: ligand-stimulated transcytosis of the polymeric immunoglobulin receptor requires two signals.Semantic proximity Read ↗

Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis.Semantic proximity Read ↗

Structural requirements for the interaction of human IgA with the human polymeric Ig receptor.Semantic proximity Read ↗

Transepithelial transport of polymeric immunoglobulins.Semantic proximity Read ↗

Vectorial transcytosis of dimeric IgA by the Calu-3 human lung epithelial cell line: upregulation by IFN-gammaSemantic proximity Read ↗

Deletions in the cytoplasmic domain of the polymeric immunoglobulin receptor differentially affect endocytotic rate and postendocytotic traffic.Semantic proximity Read ↗

Identification of a cytoplasmic signal for apical transcytosis.Semantic proximity Read ↗

Mutations within the NH2-terminal transmembrane domain of membrane immunoglobulin (Ig) M alters Ig alpha and Ig beta association and signal transduction.Semantic proximity Read ↗

Secretory Antibody Formation: Conserved Binding Interactions between J Chain and Polymeric Ig Receptor from Humans and AmphibiansSemantic proximity Read ↗

Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.