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Polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8)

Target: GALNT8
Molecular classification: Enzyme, Glycosyltransferase

Overview

Polypeptide N-acetylgalactosaminyltransferase 8 (GALNT8) is a member of the GalNAc-T family of glycosyltransferases responsible for the initial step of mucin-type O-linked glycosylation.[1][6] It transfers N-acetyl-D-galactosamine (GalNAc) to serine or threonine residues on target proteins within the Golgi apparatus, a modification affecting protein function, stability, and cellular localization.[1][6] This enzyme shows overlapping yet distinct substrate specificity compared to other GalNAc-T family members, and plays regulatory roles in post-translational modifications relevant to protein sorting and signaling.[1][6] GALNT8 has been implicated in the suppression of breast cancer cell metastasis and aberrant glycosylation-linked pathologies, including certain metabolic and neoplastic diseases.[5]

Other names: GALNAC-T8GalNAc-T8pp-GaNTase 8Polypeptide GalNAc transferase 8Protein-UDP acetylgalactosaminyltransferase 8UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 8Probable polypeptide N-acetylgalactosaminyltransferase 8

Mechanism of action

Enzyme inhibition or modulation (no specific drugs reported)

Biological functions

Initiation of O-linked glycosylationProtein post-translational modificationCarbohydrate binding

Disease associations

Cancer (notably breast cancer metastasis suppression)CalcinosisHyperphosphatemia

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