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First published online March 4, 2009

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nAChr maturation: reining in RIC-3

The biogenesis and maturation of nicotinic acetylcholine receptors (nAChRs) in neurons is a complex multi-step process. Receptor maturation is assisted by several chaperones, including RIC-3, which is active in the early stages of receptor assembly and increases the surface expression of mature receptors. Despite its role as a chaperone, elevated RIC-3 levels can be deleterious, as Millet Treinin and colleagues (p. 807) now report. Using a yeast two-hybrid screen, the authors first identify the protein BATH-42 as an interaction partner of RIC-3. They next show that, in C. elegans, loss of BATH-42 function causes RIC-3 levels to increase; bath-42 loss-of-function worms have reduced nAChR function in vulval muscle. However, the overexpression of bath-2 in adult worms is also deleterious, causing reduced pharyngeal pumping. Notably, this effect is dependent both on RIC-3 and on the CUL-3 ubiquitin ligase complex (with which BATH-42 is known to interact). BATH-42 has a similar domain structure to other CUL-3-binding proteins, which are thought to target specific proteins for ubiquitylation and proteasomal degradation; thus, the authors propose that BATH-42 might regulate RIC-3 levels in a similar way. Their data underscore the importance of regulating chaperone levels in nAChR maturation.

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Related articles in JCS:

The BTB-MATH protein BATH-42 interacts with RIC-3 to regulate maturation of nicotinic acetylcholine receptors

Anna Shteingauz, Emiliano Cohen, Yoav Biala, and Millet Treinin
JCS 2009 122: 807-812. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?