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The polymeric immunoglobulin receptor.

K Mostov1

  • 1Department of Anatomy, University of California, San Francisco 94143.

Seminars in Cell Biology
|December 1, 1991
PubMed
Summary
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The polymeric immunoglobulin receptor directs protein traffic in epithelial cells. Its cytoplasmic domain contains signals for basolateral sorting, endocytosis, and transcytosis, crucial for cellular transport.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Epithelial cells utilize complex protein traffic pathways.
  • The polymeric immunoglobulin receptor (pIgR) is a key model for studying these processes.
  • Understanding pIgR trafficking is essential for deciphering cellular transport mechanisms.

Purpose of the Study:

  • To investigate the sorting signals within the cytoplasmic domain of the polymeric immunoglobulin receptor.
  • To elucidate the molecular mechanisms governing pIgR transport in epithelial cells.

Main Methods:

  • Utilized the polymeric immunoglobulin receptor as a model system.
  • Analyzed the cytoplasmic domain of pIgR for specific sorting signals.
  • Investigated the roles of tyrosine residues and serine phosphorylation in receptor trafficking.

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Main Results:

  • Identified a 17-residue region near the membrane as an autonomous signal for basolateral sorting.
  • Discovered two distinct signals containing tyrosine residues responsible for endocytosis.
  • Demonstrated that serine phosphorylation of pIgR signals transcytosis.

Conclusions:

  • The cytoplasmic domain of pIgR contains multiple, distinct sorting signals.
  • These signals mediate sequential steps in protein traffic: basolateral localization, endocytosis, and apical transcytosis.
  • Phosphorylation and specific amino acid motifs are critical for regulated protein transport in epithelial cells.