NDLI: Identification and Functional Characterization of an N-terminal Oligomerization Domain for Polycystin-2*

Content Provider	PubMed Central
Author	Feng, Shuang Okenka, Genevieve M. Bai, Chang-xi Streets, Andrew J. Newby, Linda J. Dechant, Brett T. Tsiokas, Leonidas Obara, Tomoko Ong, Albert C. M.
Abstract	Autosomal dominant polycystic kidney disease (ADPKD), the most common inherited cause of kidney failure, is caused by mutations in either PKD1 (85%) or PKD2 (15%). The PKD2 protein, polycystin-2 (PC2 or TRPP2), is a member of the transient receptor potential (TRP) superfamily and functions as a non-selective calcium channel. PC2 has been found to form oligomers in native tissues suggesting that it may form functional homo- or heterotetramers with other subunits, similar to other TRP channels. Our experiments unexpectedly revealed that PC2 mutant proteins lacking the known C-terminal dimerization domain were still able to form oligomers and co-immunoprecipitate full-length PC2, implying the possible existence of a proximal dimerization domain. Using yeast two-hybrid and biochemical assays, we have mapped an alternative dimerization domain to the N terminus of PC2 (NT2-1-223, L224X). Functional characterization of this domain demonstrated that it was sufficient to induce cyst formation in zebrafish embryos and inhibit PC2 surface currents in mIMCD3 cells probably by a dominant-negative mechanism. In summary, we propose a model for PC2 assembly as a functional tetramer which depends on both C- and N-terminal dimerization domains. These results have significant implications for our understanding of PC2 function and disease pathogenesis in ADPKD and provide a new strategy for studying PC2 function.
Related Links	http://dx.doi.org/10.1074/jbc.m803834200
Ending Page	28479
Page Count	9
Starting Page	28471
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	42
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2008-10-17
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Identification and Functional Characterization of an N-terminal Oligomerization Domain for Polycystin-2

Identification and Functional Characterization of an N-terminal Oligomerization Domain for $Polycystin-2^{*}$

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Identification and Functional Characterization of an N-terminal Oligomerization Domain for Polycystin-2*

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