Selective modification of glycoprotein substrates by GnT-V in mouse kidney.

ABSTRACT: N-Glycans are modified by various glycosyltransferases in a protein-selective manner and critically control protein functions. Here, we investigated the mechanisms for the protein substrate selectivity of N-acetylglucosaminyltransferase-V (GnT-V or MGAT5) in the mouse kidney. Through lectin-assisted proteomics, two metalloproteases on the apical surface of tubules, alanyl aminopeptidase (ANPEP) and meprin α (MEP1A), were identified as the major GnT-V substrates. We further determined the GnT-V-modified glycosites and revealed that the modified sites are highly accessible and clustered within the C-terminal domains, suggesting some structural requirements for GnT-V action. Single-cell transcriptomics revealed partial overlap of Mgat5 and Anpep or Mep1a, ex

SUBMITTER: Osuka RF 

PROVIDER: S-EPMC12661204 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature