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Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins.
- Source :
-
The Journal of cell biology [J Cell Biol] 2004 Nov 22; Vol. 167 (4), pp. 699-709. - Publication Year :
- 2004
-
Abstract
- 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.
- Subjects :
- Animals
Cell Line
Cholesterol metabolism
Dogs
Golgi Apparatus metabolism
Macromolecular Substances metabolism
Models, Biological
Polymers metabolism
Protein Transport physiology
Cell Polarity physiology
Epithelial Cells metabolism
Glycosylphosphatidylinositols biosynthesis
Membrane Microdomains metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9525
- Volume :
- 167
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- The Journal of cell biology
- Publication Type :
- Academic Journal
- Accession number :
- 15557121
- Full Text :
- https://doi.org/10.1083/jcb.200407094