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Published 22 November 2004. doi:10.1083/jcb.200407094
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 4, 699-709
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Article

Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins



Simona Paladino1,2, Daniela Sarnataro1, Rudolf Pillich1, Simona Tivodar1, Lucio Nitsch1, and Chiara Zurzolo1,2

1 Dipartimento di Biologia e Patologia Cellulare e Molecolare, Centro di Endocrinologia ed Oncologia Sperimentale, CNR, Università degli Studi di Napoli Federico II, Italy
2 Unité de Trafic Membranaire et Pathogénèse, Institut Pasteur, 75105 Paris, France

Correspondence to Chiara Zurzolo: zurzolo{at}pasteur.fr

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.

Abbreviations used in this paper: ßCD, methyl-ß-cyclodextrin; BS3, bis(sulfosuccinimidyl)suberate; DRM, detergent-resistant membrane; DRMs, detergent-resistant microdomains; Endo H, endoglycosidase H; GH-DAF, growth hormone-decay accelerating factor; GPI, glycosylphosphatidylinositol; GPI-APs, GPI-anchored proteins; HMW, high molecular weight; PLAP, placental alkaline phosphatase; TX-100, Triton X-100.


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