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A Single Amino Acid Residue Constitutes the Third Dimerization Domain Essential for the Assembly and Function of the Tetrameric Polycystin-2 (TRPP2) Channel\* by Shuang Feng; Lise Rodat-Despoix; Patrick Delmas; Albert C.M. Ong is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is A Single Amino Acid Residue Constitutes the Third Dimerization Domain Essential for the Assembly and Function of the Tetrameric Polycystin-2 (TRPP2) Channel\* about?

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 nonselective calcium channel. PC2 has been found to form oligomers in native tissues, suggesting that similar to other TRP channels, it may form functional homo- or heterotetramers with other TRP subunits. We have recently demonstrated that the homodimerization of PC2 is mediated by both N-terminal and C-terminal domains, and it is known that PC2 can heterodimerize with PC1, TRPC1, and TRPV4. In this paper, we report that a single cysteine residue, Cys^632^, mutated in a known PKD2 pedigree, constitutes the third dimerization domain for PC2. PC2 truncation mutants lacking both N and C termini could still dimerize under nonreducing conditions. Mutation of Cys^632^ alone abolished dimerization in these mutants, indicating that it was the critical residue mediating disulfide bond formation between PC2 monomers. Co-expression of C632A PC2 mutants with wild-type PC2 channels reduced ATP-s

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Author

Shuang Feng; Lise Rodat-Despoix; Patrick Delmas; Albert C.M. Ong

Publisher

Elsevier BV

Published

2011

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)