[EN] The Lafora disease (LD, OMIM: 254780) is a progressive myoclonic epilepsy, which is characterized by a neuronal degeneration, accumulation of insoluble and poorly branched glycogen inclusion bodies (named Lafora bodies) and an imbalance in the protein homeostasis (proteostasis). STBD1 (Starch binding domain-containing protein 1) is involved in glycogen metabolism, probably in its degradation. This protein contains a carbohydrate binding domain which might have a function anchoring glycogen to membranes. Under stress conditions, such as glucose deprivation, STBD1 interacts with laforin, one of the proteins whose mutation causes the Lafora disease. In these conditions, it has also been shown that the cellular localisation of laforin changes from the citoplasm to the nucleus, in that regard it could be possible that STBD1 might act as an anchor for laforin in the cytoplasm when the stress is absent. It is also known that laforin and an E3 ubicuitin ligase, malin, the other protein whose mutation causes Lafora disease, form a functional complex. The complex promotes the ubicuitination of, amongst others, proteins involved in the glycogen metabolism, which undergo autophagy-mediated degradation. STBD1 could be a substrate of ubiquitination of the malin-laforin complex. In our work, we have demonstrated that STBD1 is a substrate of ubiquitination of this complex, and the topology of polyubiquitination is formed through lysine-63 residues of the ubicuitin molecules, which indicates that STBD1 would be degraded by autophagy modulated at least in part by the malinlaforin complex. TFGM