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Published online 20 March 2006. doi:10.1083/jcb.200507116
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 7, 1023-1034
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Article

 GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells

Simona Paladino1,2, Thomas Pocard2, Maria Agata Catino1,2, and Chiara Zurzolo1,2

1 Dipartimento di Biologia e Patologia Cellulare e Molecolare, CEINGE Biotecnologie Avanzate, Università degli Studi di Napoli Federico II, 80131 Napoli, Italy
2 Unité de Trafic Membranaire et Pathogénèse, Institut Pasteur, 75724 Paris Cedex 15, France

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

The polarity of epithelial cells is dependent on their ability to target proteins and lipids in a directional fashion. The trans-Golgi network, the endosomal compartment, and the plasma membrane act as sorting stations for proteins and lipids. The site of intracellular sorting and pathways used for the apical delivery of glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) are largely unclear. Using biochemical assays and confocal and video microscopy in living cells, we show that newly synthesized GPI-APs are directly delivered to the apical surface of fully polarized Madin–Darby canine kidney cells. Impairment of basolateral membrane fusion by treatment with tannic acid does not affect the direct apical delivery of GPI-APs, but it does affect the organization of tight junctions and the integrity of the monolayer. Our data clearly demonstrate that GPI-APs are directly sorted to the apical surface without passing through the basolateral membrane. They also reinforce the hypothesis that apical sorting of GPI-APs occurs intracellularly before arrival at the plasma membrane.

Abbreviations used in this paper: GPI, glycosylphosphatidylinositol; GPI-AP, GPI-anchored protein; NTR, neurotrophin receptor; PATJ, Pals1-associated tight junction protein; PLAP, placental alkaline phosphatase; RE, recycling endosome; TER, transepithelial resistance.


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