Ciliary membrane proteins traffic through the Golgi via a Rabep1/GGA1/Arl3-dependent mechanism

Hyunho Kim, Hangxue Xu, Qin Yao, Weizhe Li, Qiong Huang, Patricia Outeda, Valeriu Cebotaru, Marco Chiaravalli, Alessandra Boletta, Klaus Piontek, Gregory G. Germino, Edward J. Weinman, Terry Watnick and Feng Qian ()
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Hyunho Kim: University of Maryland School of Medicine
Hangxue Xu: University of Maryland School of Medicine
Qin Yao: University of Maryland School of Medicine
Weizhe Li: University of Maryland School of Medicine
Qiong Huang: University of Maryland School of Medicine
Patricia Outeda: University of Maryland School of Medicine
Valeriu Cebotaru: The Johns Hopkins University School of Medicine
Marco Chiaravalli: San Raffaele Scientific Institute
Alessandra Boletta: San Raffaele Scientific Institute
Klaus Piontek: The Johns Hopkins University School of Medicine
Gregory G. Germino: National Institute of Diabetes and Digestive and Kidney Disease, National Institute of Health
Edward J. Weinman: University of Maryland School of Medicine
Terry Watnick: University of Maryland School of Medicine
Feng Qian: University of Maryland School of Medicine

Nature Communications, 2014, vol. 5, issue 1, 1-13

Abstract: Abstract Primary cilia contain specific receptors and channel proteins that sense the extracellular milieu. Defective ciliary function causes ciliopathies such as autosomal dominant polycystic kidney disease (ADPKD). However, little is known about how large ciliary transmembrane proteins traffic to the cilia. Polycystin-1 (PC1) and -2 (PC2), the two ADPKD gene products, are large transmembrane proteins that co-localize to cilia where they act to control proper tubular diameter. Here we describe that PC1 and PC2 must interact and form a complex to reach the trans-Golgi network (TGN) for subsequent ciliary targeting. PC1 must also be proteolytically cleaved at a GPS site for this to occur. Using yeast two-hybrid screening coupled with a candidate approach, we identify a Rabep1/GGA1/Arl3-dependent ciliary targeting mechanism, whereby Rabep1 couples the polycystin complex to a GGA1/Arl3-based ciliary trafficking module at the TGN. This study provides novel insights into the ciliary trafficking mechanism of membrane proteins.

Date: 2014
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DOI: 10.1038/ncomms6482

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