RRC ID 46467
Author Wilson KJ, Qadota H, Mains PE, Benian GM.
Title 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.
Journal Mol Biol Cell
Abstract The ubiquitin proteasome system is involved in degradation of old or damaged sarcomeric proteins. Most E3 ubiquitin ligases are associated with cullins, which function as scaffolds for assembly of the protein degradation machinery. Cullin 3 uses an adaptor to link to substrates; in Caenorhabditis elegans, one of these adaptors is the BTB-domain protein MEL-26 (maternal effect lethal). Here we show that MEL-26 interacts with the giant sarcomeric protein UNC-89 (obscurin). MEL-26 and UNC-89 partially colocalize at sarcomeric M-lines. Loss of function or gain of function of mel-26 results in disorganization of myosin thick filaments similar to that found in unc-89 mutants. It had been reported that in early C. elegans embryos, a target of the CUL-3/MEL-26 ubiquitylation complex is the microtubule-severing enzyme katanin (MEI-1). Loss of function or gain of function of mei-1 also results in disorganization of thick filaments similar to unc-89 mutants. Genetic data indicate that at least some of the mel-26 loss-of-function phenotype in muscle can be attributed to increased microtubule-severing activity of MEI-1. The level of MEI-1 protein is reduced in an unc-89 mutant, suggesting that the normal role of UNC-89 is to inhibit the CUL-3/MEL-26 complex toward MEI-1.
Volume 23(14)
Pages 2623-34
Published 2012-7-1
DOI 10.1091/mbc.E12-01-0055
PII mbc.E12-01-0055
PMID 22621901
PMC PMC3395652
MeSH Adaptor Proteins, Signal Transducing / genetics Adaptor Proteins, Signal Transducing / metabolism* Adenosine Triphosphatases / genetics Adenosine Triphosphatases / metabolism* Animals Animals, Genetically Modified Caenorhabditis elegans / embryology Caenorhabditis elegans / genetics Caenorhabditis elegans / metabolism* Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Cullin Proteins / metabolism Muscle Proteins / genetics Muscle Proteins / metabolism* Muscle, Striated / metabolism* Myosins / metabolism Proteolysis RNA Interference RNA, Small Interfering Sarcomeres / metabolism Ubiquitin / metabolism Ubiquitin-Protein Ligases / metabolism Ubiquitination
IF 3.791
Times Cited 24
WOS Category CELL BIOLOGY
Resource
C.elegans tm752