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Isoform differences drive functional diversity of NHR-49
Lexus Tatge1, Peter M Douglas1,2
1Molecular Biology, The University of Texas Southwestern Medical Center, Dallas, Texas, United States.
Micropublication Biology
|August 19, 2025
Summary
The nuclear hormone receptor NHR-49 in C. elegans has distinct isoforms affecting lipid metabolism. This study reveals isoform-specific localization and protein interactions, adding complexity to nuclear receptor regulation.
Area of Science:
- Molecular Biology
- Cell Biology
- Genetics
Background:
- The nuclear hormone receptor NHR-49 regulates lipid metabolism in *C. elegans*.
- NHR-49 exists in five isoforms with differing N-termini, but their functional distinctions are poorly understood.
Purpose of the Study:
- To investigate the functional differences between NHR-49 isoforms.
- To explore the subcellular localization and protein interaction networks of NHR-49 isoforms.
Main Methods:
- CRISPR-based N- and C-terminal epitope tagging using TurboID for proximity labeling.
- Analysis of subcellular localization dynamics.
- Identification of protein interactomes for different NHR-49 isoforms.
Main Results:
- The longest NHR-49 isoform exhibits dynamic subcellular localization between the nucleus and cytoplasm.
- N-terminally tagged NHR-49 isoform interacts with cytoplasmic proteins, including endocytic machinery (RAB-10, RAB-11.1).
- C-terminally tagged NHR-49 isoform associates with nuclear pore components and transcriptional regulators.
Conclusions:
- NHR-49 isoforms display distinct subcellular localization and interactomes.
- Isoform-specific differences in NHR-49 significantly impact its regulatory functions.
- Understanding isoform preferences is crucial for interpreting functional genomics data in *C. elegans* and other organisms.
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