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Structural characterization of life-extending Caenorhabditis elegans Lipid Binding Protein 8
- Source :
- Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019), Scientific Reports
- Publication Year :
- 2019
- Publisher :
- Springer Science and Business Media LLC, 2019.
-
Abstract
- The lysosome plays a crucial role in the regulation of longevity. Lysosomal degradation is tightly coupled with autophagy that is induced by many longevity paradigms and required for lifespan extension. The lysosome also serves as a hub for signal transduction and regulates longevity via affecting nuclear transcription. One lysosome-to-nucleus retrograde signaling pathway is mediated by a lysosome-associated fatty acid binding protein LBP-8 in Caenorhabditis elegans. LBP-8 shuttles lysosomal lipids into the nucleus to activate lipid regulated nuclear receptors NHR-49 and NHR-80 and consequently promote longevity. However, the structural basis of LBP-8 action remains unclear. Here, we determined the first 1.3 Å high-resolution structure of this life-extending protein LBP-8, which allowed us to identify a structurally conserved nuclear localization signal and amino acids involved in lipid binding. Additionally, we described the range of fatty acids LBP-8 is capable of binding and show that it binds to life-extending ligands in worms such as oleic acid and oleoylethanolamide with high affinity.
- Subjects :
- 0301 basic medicine
Longevity
lcsh:Medicine
Helix-turn-helix
Fatty Acid-Binding Proteins
Article
Fatty acid-binding protein
03 medical and health sciences
0302 clinical medicine
Lysosome
medicine
Animals
Amino Acid Sequence
Caenorhabditis elegans
Caenorhabditis elegans Proteins
lcsh:Science
Helix-Turn-Helix Motifs
X-ray crystallography
Cell Nucleus
Multidisciplinary
biology
Chemistry
Fatty Acids
lcsh:R
Autophagy
biology.organism_classification
Cell biology
Ageing
030104 developmental biology
medicine.anatomical_structure
Retrograde signaling
lcsh:Q
Intracellular signalling peptides and proteins
Signal transduction
Lysosomes
030217 neurology & neurosurgery
Nuclear localization sequence
Molecular Chaperones
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 9
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....34eea5b63a7702827a28947fd8f5454e