Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells

E. Wang, J. G. Pennington, J. R. Goldenring, W. Hunziker, K. W. Dunn

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


Recent studies showing thorough intermixing of apical and basolateral endosomes have demonstrated that endocytic sorting is critical to maintaining the plasma membrane polarity of epithelial cells. Our studies of living, polarized cells show that disrupting endocytosis with brefeldin-A rapidly destroys the polarity of transferrin receptors in MDCK cells while having no effect on tight junctions. Brefeldin-A treatment induces tubulation of endosomes, but the sequential compartments and transport steps of the transcytotic pathway remain intact. Transferrin is sorted from LDL, but is then missorted from common endosomes to the apical recycling endosome, as identified by its nearly neutral pH, and association with GFP chimeras of Rabs 11a and 25. From the apical recycling endosome, transferrin is then directed to the apical plasma membrane. These data are consistent with a model in which polarized sorting of basolateral membrane proteins occurs via a brefeldin-A-sensitive process of segregation into basolateral recycling vesicles. Although disruption of polar sorting correlates with dissociation of γ-adaptin from endosomes, γ-adaptin does not appear to be specifically involved in sorting into recycling vesicles, as we find it associated with the transcytotic pathway, and particularly to the post-sorting transcytotic apical recycling endosome.

Original languageEnglish (US)
Pages (from-to)3309-3321
Number of pages13
JournalJournal of cell science
Issue number18
StatePublished - 2001
Externally publishedYes


  • Endocytosis
  • Epithelium
  • MDCK cell
  • Polarity
  • Transferrin

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells'. Together they form a unique fingerprint.

Cite this