ArticleMolecular biology of the cell1998
Role of tyrosine phosphorylation in ligand-induced regulation of transcytosis of the polymeric Ig receptor.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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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.
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Who cites it
16 citing papers in PubMed, 48 citations in OpenAlex.
- A new look at transudation: the apocrine connection.Physiological research · 2020Review
- Regulation of the polymeric immunoglobulin receptor and IgA transport: new advances in environmental factors that stimulate pIgR expression and its role in mucosal immunity.Mucosal immunology · 2011Review
- A kinase cascade leading to Rab11-FIP5 controls transcytosis of the polymeric immunoglobulin receptor.Nature cell biology · 2010Article
- Polymeric immunoglobulin receptor-mediated invasion of Streptococcus pneumoniae into host cells requires a coordinate signaling of SRC family of protein-tyrosine kinases, ERK, and c-Jun N-terminal kinase.The Journal of biological chemistry · 2010Article
- Identification of a cytoplasmic signal for apical transcytosis.Traffic (Copenhagen, Denmark) · 2009Article
- Cdc42 and the phosphatidylinositol 3-kinase-Akt pathway are essential for PspC-mediated internalization of pneumococci by respiratory epithelial cells.The Journal of biological chemistry · 2009Article
- Cholesterol-sensitive modulation of transcytosis.Molecular biology of the cell · 2007Article
- Phosphoinositide 3-kinase regulates the role of retromer in transcytosis of the polymeric immunoglobulin receptor.Experimental cell research · 2007Article
- Rotavirus anti-VP6 secretory immunoglobulin A contributes to protection via intracellular neutralization but not via immune exclusion.Journal of virology · 2006Article
- Antibodies to the polymeric immunoglobulin receptor with different binding and trafficking patterns.American journal of respiratory cell and molecular biology · 2005Article
- Transcytosis of NgCAM in epithelial cells reflects differential signal recognition on the endocytic and secretory pathways.The Journal of cell biology · 2005Article
- Uncovering multiple axonal targeting pathways in hippocampal neurons.The Journal of cell biology · 2003Article
- Exocyst is involved in cystogenesis and tubulogenesis and acts by modulating synthesis and delivery of basolateral plasma membrane and secretory proteins.Molecular biology of the cell · 2000Article
- The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoform.Molecular biology of the cell · 2000Article
- Polarized sphingolipid transport from the subapical compartment changes during cell polarity development.Molecular biology of the cell · 2000Article
- Transduction of basolateral-to-apical signals across epithelial cells: ligand-stimulated transcytosis of the polymeric immunoglobulin receptor requires two signals.Molecular biology of the cell · 1999Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The polymeric Ig receptor (pIgR) transcytoses its ligand, dimeric IgA (dIgA), from the basolateral to the apical surface of epithelial cells. Although the pIgR is constitutively transcytosed in the absence of ligand, binding of dIgA stimulates transcytosis of the pIgR. We recently reported that dIgA binding to the pIgR induces translocation of protein kinase C, production of inositol triphosphate, and elevation of intracellular free calcium. We now report that dIgA binding causes rapid, transient tyrosine phosphorylation of several proteins, including phosphatidyl inositol-specific phospholipase C-gammal. Protein tyrosine kinase inhibitors or deletion of the last 30 amino acids of pIgR cytoplasmic tail prevents IgA-stimulated protein tyrosine kinase activation, tyrosine phosphorylation of phospholipase C-gammal, production of inositol triphosphate, and the stimulation of transcytosis by dIgA. Analysis of pIgR deletion mutants reveals that the same discrete portion of the cytoplasmic domain, residues 727-736 (but not the Tyr734), controls both the ability of pIgR to cause dIgA-induced tyrosine phosphorylation of the phospholipase C-gammal and to undergo dIgA-stimulated transcytosis. In addition, dIgA transcytosis can be strongly stimulated by mimicking phospholipase C-gammal activation. In combination with our previous results, we conclude that the protein tyrosine kinase(s) and phospholipase C-gammal that are activated upon dIgA binding to the pIgR control dIgA-stimulated pIgR transcytosis.
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Registered trials
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.