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Cited by 282

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif

Geng, Lin, Okuhara, Dayne, Yu, Zhiheng, Tian, Xin, Cai, Yiqiang, Shibazaki, Sekiya, Somlo, Stefan·2006·Journal of Cell Science

Abstract

Primary cilia play a key role in the pathogenesis of autosomal dominant polycystic kidney disease (ADPKD). The affected proteins, polycystin-1 (PC1) and polycystin-2 (PC2), interact with each other and are expressed in cilia. We found that COOH-terminal truncated PC2 (PC2-L703X), lacking the PC1 interaction region, still traffics to cilia. We examined PC2 expression in several tissues and cells lacking PC1 and found that PC2 is expressed in cilia independently of PC1. We used N-terminal deletion constructs to narrow the domain necessary for cilia trafficking to the first 15 amino acids of PC2 and identified a conserved motif, R6VxP, that is required for cilial localization. The N-terminal 15 amino acids are also sufficient to localize heterologous proteins in cilia. PC2 has endogenous cilia trafficking information and is present in cilia of cells lining cysts that result from mutations in PKD1.

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Metadata

Authors
Geng, L., Okuhara, D., Yu, Z., Tian, X., Cai, Y., Shibazaki, S., & Somlo, S.
Venue
Journal of Cell Science
Published
2006-04-01
Volume
119
Issue
7
Pages
1383-1395
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
OpenAlex
W1959400241
Cited by
282
References
5
FWCI
11.13
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif. https://app.cochat.ai/papers/10.1242/jcs.02818
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Geng, L., Okuhara, D., Yu, Z., Tian, X., Cai, Y., Shibazaki, S., & Somlo, S. (2006). Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif. Journal of Cell Science. https://doi.org/10.1242/jcs.02818

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