ArticleBioscience reports2014
The carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactions.
Article in Bioscience reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- Glycophagy is an ancient bilaterian pathway supporting metabolic adaptation through STBD1 structural evolution.Communications biology · 2026Article
- Glycophagy: molecular mechanisms, regulatory signals, and disease associations.Autophagy reports · 2026Review
- Alzheimer's disease brain-derived tau extracts show differential processing and transcriptional effects in human astrocytes.iScience · 2025Article
- Structural and biochemical insight into a modular β-1,4-galactan synthase in plants.Nature plants · 2023Article
- Review
- Genetic loss of AMPK-glycogen binding destabilises AMPK and disrupts metabolism.Molecular metabolism · 2020Article
- Stbd1 promotes glycogen clustering during endoplasmic reticulum stress and supports survival of mouse myoblasts.Journal of cell science · 2020Article
- Biomedical Implications of Autophagy in Macromolecule Storage Disorders.Frontiers in cell and developmental biology · 2019Review
- Lafora disease: from genotype to phenotype.Journal of genetics · 2018Review
- Cargo recognition and degradation by selective autophagy.Nature cell biology · 2018Review
- Article
- Mouse Stbd1 isJournal of cell science · 2017Article
- Autophagy in the liver: functions in health and disease.Nature reviews. Gastroenterology & hepatology · 2017Review
- Starch Binding Domain-containing Protein 1 Plays a Dominant Role in Glycogen Transport to Lysosomes in Liver.The Journal of biological chemistry · 2016Article
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Loss of protein targeting to glycogen sensitizes human hepatocellular carcinoma cells towards glucose deprivation mediated oxidative stress and cell death.Bioscience reports · 2015Article
- Changing shapes of glycogen-autophagy nexus in neurons: perspective from a rare epilepsy.Frontiers in neurology · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
STBD1 (starch-binding domain-containing protein 1) belongs to the CBM20 (family 20 carbohydrate binding module) group of proteins, and is implicated in glycogen metabolism and autophagy. However, very little is known about its regulation or interacting partners. Here, we show that the CBM20 of STBD1 is crucial for its stability and ability to interact with glycogen-associated proteins. Mutation of a conserved tryptophan residue (W293) in this domain abolished the ability of STBD1 to bind to the carbohydrate amylose. Compared with the WT (wild-type) protein, this mutant exhibited rapid degradation that was rescued upon inhibition of the proteasome. Furthermore, STBD1 undergoes ubiquitination when expressed in COS cells, and requires the N-terminus for this process. In contrast, inhibition of autophagy did not significantly affect protein stability. In overexpression experiments, we discovered that STBD1 interacts with several glycogen-associated proteins, such as GS (glycogen synthase), GDE (glycogen debranching enzyme) and Laforin. Importantly, the W293 mutant of STBD1 was unable to do so, suggesting an additional role for the CBM20 domain in protein-protein interactions. In HepG2 hepatoma cells, overexpressed STBD1 could associate with endogenous GS. This binding increased during glycogenolysis, suggesting that glycogen is not required to bridge this interaction. Taken together, our results have uncovered new insights into the regulation and binding partners of STBD1.
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