Co-assembly of polycystin-1 and -2 produces unique cation-permeable currents

Kazushige Hanaoka, Feng Qian, Alessandra Boletta, Anil K. Bhunia, Klaus Piontek, Leonidas Tsiokas, Vikas P. Sukhatme, William B. Guggino () and Gregory G. Germino ()
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Kazushige Hanaoka: Department of Physiology
Feng Qian: Johns Hopkins University School of Medicine
Alessandra Boletta: Johns Hopkins University School of Medicine
Anil K. Bhunia: Johns Hopkins University School of Medicine
Klaus Piontek: Johns Hopkins University School of Medicine
Leonidas Tsiokas: University of Oklahoma Health Science Center
Vikas P. Sukhatme: Beth Israel Deaconess Medical Center, Harvard Medical School
William B. Guggino: Department of Physiology
Gregory G. Germino: Johns Hopkins University School of Medicine

Nature, 2000, vol. 408, issue 6815, 990-994

Abstract: Abstract The human kidney is composed of roughly 1.2-million renal tubules that must maintain their tubular structure to function properly. In autosomal dominant polycystic kidney disease (ADPKD) cysts develop from renal tubules and enlarge independently, in a process that ultimately causes renal failure in 50% of affected individuals1,2. Mutations in either PKD1 or PKD2 are associated with ADPKD but the function of these genes is unknown. PKD1 is thought to encode a membrane protein, polycystin-1, involved in cell–cell or cell–matrix interactions3,4,5, whereas the PKD2 gene product, polycystin-2, is thought to be a channel protein6. Here we show that polycystin-1 and -2 interact to produce new calcium-permeable non-selective cation currents. Neither polycystin-1 nor -2 alone is capable of producing currents. Moreover, disease-associated mutant forms of either polycystin protein that are incapable of heterodimerization do not result in new channel activity. We also show that polycystin-2 is localized in the cell in the absence of polycystin-1, but is translocated to the plasma membrane in its presence. Thus, polycystin-1 and -2 co-assemble at the plasma membrane to produce a new channel and to regulate renal tubular morphology and function.

Date: 2000
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DOI: 10.1038/35050128

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