Oglykosylácii

Oglykosylácii, also known as O-glycosylation, is a post-translational modification where sugar moieties are covalently attached to the hydroxyl groups of serine, threonine, or tyrosine residues in proteins. This process differs from N-glycosylation, which targets asparagine residues. O-glycosylation primarily occurs in the Golgi apparatus, with glycosyltransferases catalyzing the transfer of sugar units from nucleotide-sugar donors to the target amino acid. It can generate diverse structures, such as mucin-type O-glycans, heavily O-glycosylated proteins abundant in mucosal tissues.

Biologically, Oglykosylácii is vital for cell-cell adhesion, immune response modulation, and signal transduction. Dysregulation of this modification is linked to diseases like cancer, where abnormal glycosylation patterns influence tumor behavior and metastasis. Research into Oglykosylácii enhances understanding of protein function and disease mechanisms, guiding therapeutic strategies.