An essential but insufficient step for apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) in epithelial cells is their association with detergent-resistant microdomains (DRMs) or rafts. In this paper, we show that in MDCK cells both apical and basolateral GPI-APs associate with DRMs during their biosynthesis. However, only apical and not basolateral GPI-APs are able to oligomerize into high molecular weight complexes. Protein oligomerization begins in the medial Golgi, concomitantly with DRM association, and is dependent on protein–protein interactions. Impairment of oligomerization leads to protein missorting. We propose that oligomerization stabilizes GPI-APs into rafts and that this additional step is required for apical sorting of GPI-APs. Two alternative apical sorting models are presented.
Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
S. Paladino,Daniela Sarnataro,R. Pillich,S. Tivodar,L. Nitsch,C. Zurzolo
Published 2004 in Journal of Cell Biology
ABSTRACT
PUBLICATION RECORD
- Publication year
2004
- Venue
Journal of Cell Biology
- Publication date
2004-11-22
- Fields of study
Biology, Medicine
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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