Extracellular heparan sulfate proteoglycans and glycan-binding lectins orchestrate trans-synaptic signaling.

ABSTRACT: The exceedingly narrow synaptic cleft (<20 nm) and adjacent perisynaptic extracellular space contain an astonishing array of secreted and membrane-anchored glycoproteins. A number of these extracellular molecules regulate intercellular trans-synaptic signaling by binding to ligands, acting as co-receptors or modulating ligand-receptor interactions. Recent work has greatly expanded our understanding of extracellular proteoglycan and glycan-binding lectin families as key regulators of intercellular signaling at the synapse. These secreted proteins act to regulate the compartmentalization of glycoprotein ligands and receptors, crosslink dynamic extracellular and cell surface lattices, modulate both exocytosis and endocytosis vesicle cycling, and control postsynaptic receptor trafficking. Here

SUBMITTER: Rushton E 

PROVIDER: S-EPMC7438005 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature