Regulated spatial organization and sensitivity of cytosolic protein oxidation in Caenorhabditis elegans

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Regulated spatial organization and sensitivity of cytosolic protein oxidation in Caenorhabditis elegans

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Title: Regulated spatial organization and sensitivity of cytosolic protein oxidation in Caenorhabditis elegans
Author: Romero-Aristizabal, Catalina; Marks, Debora S.; Fontana, Walter; Apfeld, Javier

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Citation: Romero-Aristizabal, Catalina, Debora S. Marks, Walter Fontana, and Javier Apfeld. 2014. “Regulated spatial organization and sensitivity of cytosolic protein oxidation in Caenorhabditis elegans.” Nature communications 5 (1): 5020. doi:10.1038/ncomms6020. http://dx.doi.org/10.1038/ncomms6020.
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Abstract: Cells adjust their behavior in response to redox events by regulating protein activity through the reversible formation of disulfide bridges between cysteine thiols. However, the spatial and temporal control of these modifications remains poorly understood in multicellular organisms. Here, we measured the protein thiol-disulfide balance in live C. elegans using a genetically-encoded redox sensor and found that it is specific to tissues and patterned spatially within a tissue. Insulin signaling regulates the sensor's oxidation at both of these levels. Unexpectedly, we found that isogenic individuals exhibit large differences in the sensor's thiol-disulfide balance. This variation contrasts with the general view that glutathione acts as the main cellular redox buffer. Indeed, our work suggests that glutathione converts small changes in its oxidation level into large changes in its redox potential. We therefore propose that glutathione facilitates the sensitive control of the thioldisulfide balance of target proteins in response to cellular redox events.
Published Version: doi:10.1038/ncomms6020
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4181376/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:14351311
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