UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans

• Type of Material: Article
• Authors: Kristy J. Wilson, Emory University; Hiroshi Qadota, Emory University; Paul E. Mains, University of Calgary; Guy Benian, Emory University
• Language: English
• Date: 2012-07-15
• Publisher: The American Society for Cell Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2012 Wilson et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).
• License: Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported
• Final Published Version (URL): http://dx.doi.org/10.1091%2Fmbc.E12-01-0055
• Title of Journal or Parent Work: Molecular Biology of the Cell
• Volume: 23
• Issue: 14
• Start Page: 2623
• End Page: 2634
• Grant/Funding Information: Some of the strains used in this work were provided by the Caenorhabditis Genetics Center (funded by the National Institutes of Health, Center for Research Resources).; We also acknowledge a Fellowship in Research and Science Teaching Postdoctoral Fellowship (K12GM000680) from the National Institutes of Health (for K.J.W.) and support from National Institutes of Health Grant R01AR051466.; P.E.M. was supported by a grant from the Canadian Institutes of Health Research.
• Research Categories: Health Sciences, Pathology

Abstract

UNC-89 (obscurin) interacts with MEL-26, a BTB-domain protein/adaptor for cullin-3. MEL-26 colocalizes with UNC-89 at M-lines. Mutations in MEL-26, CUL-3 (cullin-3), and MEI-1 (katanin) result in a muscle phenotype similar to that of unc-89 mutants. The level of MEI-1 is reduced in unc-89 mutants, suggesting that normally UNC-89 inhibits CUL-3/MEL-26 in muscle.