Skip to Main content Skip to Navigation
Journal articles

Oligomerization is a specific requirement for apical sorting of glycosyl-phosphatidylinositol-anchored proteins but not for non-raft-associated apical proteins.

Abstract : Protein apical sorting in polarized epithelial cells is mediated by two different mechanisms, raft dependent and raft independent. In Madin-Darby canine kidney (MDCK) cells, an essential step for apical sorting of glycosyl-phosphatidylinositol (GPI)-anchored proteins (GPI-APs) is their coalescence into high-molecular-weight (HMW) oligomers. Here we show that this mechanism is also functional in Fischer rat thyroid cells, which possess a different sorting phenotype compared with MDCK cells. We demonstrate that, as in MDCK cells, both apical and basolateral GPI-APs associate with detergent-resistant microdomains, but that only the apical proteins are able to oligomerize into HMW complexes during their passage through the medial Golgi. We also show that oligomerization is a specific requirement for apical sorting of GPI-APs and is not used by transmembrane, non-raft-associated apical proteins.
Document type :
Journal articles
Complete list of metadatas

https://hal-pasteur.archives-ouvertes.fr/pasteur-00166611
Contributor : Christiane Goisnard <>
Submitted on : Tuesday, August 7, 2007 - 4:41:08 PM
Last modification on : Friday, September 18, 2020 - 2:52:03 PM

Links full text

Identifiers

Collections

Citation

Simona Paladino, Daniela Sarnataro, Simona Tivodar, Chiara Zurzolo. Oligomerization is a specific requirement for apical sorting of glycosyl-phosphatidylinositol-anchored proteins but not for non-raft-associated apical proteins.. Traffic, Wiley, 2007, 8 (3), pp.251-8. ⟨10.1111/j.1600-0854.2006.00522.x⟩. ⟨pasteur-00166611⟩

Share

Metrics

Record views

192