Version 1
: Received: 26 September 2024 / Approved: 27 September 2024 / Online: 27 September 2024 (15:30:52 CEST)
How to cite:
Wijewantha, N. V.; Battu, P.; Chen, K.; Kumar, R.; Nazarko, T. Y. New Toolset of Reporters Reveals That Glycogen Granules Are Neutral Substrates of Bulk Autophagy in Komagataella phaffii. Preprints2024, 2024092233. https://doi.org/10.20944/preprints202409.2233.v1
Wijewantha, N. V.; Battu, P.; Chen, K.; Kumar, R.; Nazarko, T. Y. New Toolset of Reporters Reveals That Glycogen Granules Are Neutral Substrates of Bulk Autophagy in Komagataella phaffii. Preprints 2024, 2024092233. https://doi.org/10.20944/preprints202409.2233.v1
Wijewantha, N. V.; Battu, P.; Chen, K.; Kumar, R.; Nazarko, T. Y. New Toolset of Reporters Reveals That Glycogen Granules Are Neutral Substrates of Bulk Autophagy in Komagataella phaffii. Preprints2024, 2024092233. https://doi.org/10.20944/preprints202409.2233.v1
APA Style
Wijewantha, N. V., Battu, P., Chen, K., Kumar, R., & Nazarko, T. Y. (2024). New Toolset of Reporters Reveals That Glycogen Granules Are Neutral Substrates of Bulk Autophagy in Komagataella phaffii. Preprints. https://doi.org/10.20944/preprints202409.2233.v1
Chicago/Turabian Style
Wijewantha, N. V., Ravinder Kumar and Taras Y. Nazarko. 2024 "New Toolset of Reporters Reveals That Glycogen Granules Are Neutral Substrates of Bulk Autophagy in Komagataella phaffii" Preprints. https://doi.org/10.20944/preprints202409.2233.v1
Abstract
Glycogen, a branched polysaccharide organized into glycogen granules (GGs), is delivered from the cytoplasm to the lysosomes of hepatocytes by the STBD1-driven selective autophagy (glycophagy). Recently, we developed Komagataella phaffii yeast as a simple model of GG autophagy and found that it proceeds non-selectively under nitrogen starvation conditions. However, another group, using Saccharomyces cerevisiae as a model, found that glycogen is a non-preferred cargo of the nitrogen-starvation induced bulk autophagy. To clarify cargo characteristics of K. phaffii GGs, we used the same glycogen synthase-based reporter (Gsy1-GFP) of GG autophagy in K. phaffii, as was used in S. cerevisiae. The K. phaffii Gsy1-GFP marked GGs and reported on their autophagic degradation during nitrogen starvation, as expected. However, unlike in S. cerevisiae, glycogen synthase-marked GGs were delivered to the vacuole and degraded there with the same efficiency as a cytosolic glycogen synthase in glycogen-deficient cells suggesting that glycogen is a neutral cargo of bulk autophagy in K. phaffii. We verified our findings with a new set of reporters based on the glycogen-binding CBM20 domain of human STBD1. The GFP-CBM20 and mCherry-CBM20 fusion proteins tagged GGs, reported about autophagy of GGs and confirmed that GGs in K. phaffii are neither preferred, nor non-preferred substrates of bulk autophagy. They are its neutral substrates.
Biology and Life Sciences, Cell and Developmental Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
