Multiple N-linked glycosylation sites critically modulate the synaptic abundance of neuroligin isoforms.

ABSTRACT: In recent years, elegant glycomic and glycoproteomic approaches have revealed an intricate glycosylation profile of mammalian brain with enormous spatial and temporal diversities. Nevertheless, at a cellular level, it is unclear how these post-translational modifications affect various proteins to influence crucial neuronal properties. Here, we have investigated the impact of N-linked glycosylation on neuroligins (NLGNs), a class of cell-adhesion molecules that play instructive roles in synapse organization. We found that endogenous NLGN proteins are differentially glycosylated across several regions of murine brain in a sex-independent but isoform-dependent manner. In both rodent primary neurons derived from brain sections and human neurons differentiated from stem cells, all NLGN variant

SUBMITTER: Benner O 

PROVIDER: S-EPMC10679506 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature