1. The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.
- Author
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Serrano MV, Cottier S, Wang L, Moreira-Antepara S, Nzessi A, Liu Z, Williams B, Lee M, Schneiter R, and Liu J
- Subjects
- Animals, Protein Domains, Protein Binding, Caenorhabditis elegans metabolism, Caenorhabditis elegans genetics, Caenorhabditis elegans Proteins metabolism, Caenorhabditis elegans Proteins genetics, Caenorhabditis elegans Proteins chemistry, Signal Transduction, Body Size, Bone Morphogenetic Proteins metabolism, Bone Morphogenetic Proteins genetics
- Abstract
The CAP (cysteine-rich secretory proteins, antigen-5, and pathogenesis-related) proteins are widely expressed and have been implicated to play diverse roles ranging from mammalian reproduction to plant immune response. Increasing evidence supports a role of CAP proteins in lipid binding. The Caenorhabditis elegans CAP protein LON-1 is known to regulate body size and bone morphogenetic protein (BMP) signaling. LON-1 is a secreted protein with a conserved CAP domain and a C-terminal unstructured domain with no homology to other proteins. In this study, we report that the C-terminal domain of LON-1 is dispensable for its function. Instead, key conserved residues located in the CAP domain are critical for LON-1 function in vivo. We further showed that LON-1 is capable of binding sterol, but not fatty acid, in vitro, and that certain key residues implicated in LON-1 function in vivo are also important for LON-1 sterol binding in vitro. These findings suggest a role of LON-1 in regulating body size and BMP signaling via sterol binding., Competing Interests: Conflicts of interest: The author(s) declare no conflict of interest., (© The Author(s) 2024. Published by Oxford University Press on behalf of The Genetics Society of America. All rights reserved. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.)
- Published
- 2025
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