STBD1 (starch binding domain 1) functions as a selective autophagy receptor that mediates glycophagy, the autophagic degradation of glycogen 1. The protein contains a carbohydrate-binding module 20 (CBM20) domain with two distinct oligosaccharide-binding sites that enable specific recognition and binding to glycogen 2. STBD1 also possesses an LC3-interacting region (LIR) motif that selectively binds to all six mammalian ATG8 family proteins, particularly GABARAPL1, facilitating the delivery of glycogen to autophagosomes 23. The protein localizes to the endoplasmic reticulum membrane and ER-mitochondria contact sites through N-myristoylation, which is crucial for its subcellular targeting 45. Beyond glycophagy, STBD1 regulates ER-mitochondrial associations and has emerged as a component of lipid droplets, mediating crosstalk between glycogen and lipid metabolism 46. Functionally, STBD1 activates AMPK signaling and enhances insulin sensitivity, suggesting protective roles in metabolic homeostasis 5. Dysregulation of STBD1 is implicated in various diseases including cardiovascular disease, metabolic disorders, and cancer, highlighting its potential as a therapeutic target 16.