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Syntaxin 17, an ancient SNARE paralog, plays different and conserved roles in different organisms
Shun Kato1, Kohei Arasaki1, Natsuki Tokutomi1
1School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
Journal of Cell Science
|October 27, 2021
Summary
Syntaxin 17 (Stx17) proteins in flies and nematodes have evolved distinct functions. Fly Stx17 aids autophagy, while nematode Stx17 facilitates mitochondrial division, revealing evolutionary divergence.
Area of Science:
- Cell Biology
- Evolutionary Biology
- Molecular Biology
Background:
- Mammalian syntaxin 17 (Stx17) is involved in membrane fusion, mitochondrial division, and autophagosome formation.
- Stx17 possesses a unique C-terminal hydrophobic region and tail, distinguishing it from conventional syntaxins.
- Stx17 is an ancient SNARE protein found across eukaryotes but has been lost in some lineages.
Purpose of the Study:
- To compare the localization and function of fly and nematode Stx17 in HeLa cells against human Stx17.
- To investigate the evolutionary divergence of Stx17 functions in metazoans.
Main Methods:
- Expression of fly and nematode Stx17 in HeLa cells.
- Localization studies of Stx17 proteins.
- Functional assays for autophagy and mitochondrial division.
Main Results:
- Fly Stx17 localized to the cytosol, mediating autophagy but not mitochondrial division.
- Nematode Stx17 localized to mitochondria, facilitating mitochondrial division but not autophagy.
- Differences in Stx17 function correlate with variations in their C-terminal tail structures.
Conclusions:
- Stx17 has evolved distinct roles in autophagy and mitochondrial division across different metazoan lineages.
- The C-terminal tail structure of Stx17 is a key determinant of its functional specialization.
- This study offers insights into the evolutionary trajectory of Stx17 in metazoans.
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