Background: LEV-9 is an extracellular scaffolding protein required for synaptic clustering of acetylcholine receptors in C. elegans. Results: C-terminal cleavage of LEV-9 is necessary for its synaptic function. Conclusion: LEV-9 is activated by proteolytic cleavage following the final tandem complement control protein (CCP) modules. Significance: Many LEV-9-related factors are likely cleaved after CCP domains, suggesting that cleavage location can be conserved in distant architecturally related proteins. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Briseno-Roa, L., & Bessereau, J. L. (2014). Proteolytic processing of the extracellular scaffolding protein lev-9 is required for clustering acetylcholine receptors. Journal of Biological Chemistry, 289(16), 10967–10974. https://doi.org/10.1074/jbc.C113.534677
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