<p>Obesity and its related metabolic diseases have increasingly become a significant public health challenge threatening the health of populations worldwide. The pathophysiological mechanisms contributing to the progression of obesity are intricate and diverse, highlighting the need for the creation of novel and effective intervention strategies aimed at the treatment of obesity and its associated metabolic diseases. An increasing number of studies indicate that glycosylation modifications play a crucial role in the onset and progression of obesity and its complications. Studies on glycosylation not only reveal its involvement in regulating the mechanisms of obesity and its complications but also provide new avenues for targeted therapies. Although significant advancements have been made in understanding the fundamental molecular mechanisms by which glycosylation modifications affect obesity and its related complications, many questions remain unanswered. For instance, through which specific sites does glycosylation regulate the occurrence of obesity and its complications? Furthermore, do glycosylation modifications interact with other post-translational modifications (PTMs) of proteins in the regulation of obesity and its complications? What are the specific pathways of O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in obesity and its complications? This article summarizes recent research on the role of glycosylation in obesity and its complications, lists relevant specific glycosylation sites, and discusses the interactions between glycosylation modifications and other PTMs of proteins, providing new perspectives and insights for clinical treatment of obesity and its complications.</p> Graphical Abstract <p></p>