title: The multi-tasked life of GM1 ganglioside, a true factotum of nature.
abstract: GM1 ganglioside occurs widely in vertebrate tissues, where it exhibits many essential functions, both in the plasma membrane and intracellular loci. Its essentiality is revealed in the dire consequences resulting from genetic deletion. This derives from its key roles in several signalosome systems, characteristically located in membrane rafts, where it associates with specific proteins that have glycolipid-binding domains. Thus, GM1 interacts with proteins that modulate mechanisms such as ion transport, neuronal differentiation, G protein-coupled receptors (GPCRs), immune system reactivities, and neuroprotective signaling. The latter occurs through intimate association with neurotrophin receptors, which has relevance to the etiopathogenesis of neurodegenerative diseases and potential therapies. Here, we review the current state of knowledge of these GM1-associated mechanisms.
authors.affiliation: Department of Neurology and Neurosciences, New Jersey Medical School, Rutgers, The State University of New Jersey, 185 South Orange Avenue, Newark, NJ 07103, USA. Electronic address: ledeenro@njms.rutgers.edu.
authors.forename: Robert W
authors.initials: RW
authors.lastname: Ledeen
authors.affiliation: Department of Neurology and Neurosciences, New Jersey Medical School, Rutgers, The State University of New Jersey, 185 South Orange Avenue, Newark, NJ 07103, USA.
authors.forename: Gusheng
authors.initials: G
authors.lastname: Wu
mesh_terms: D000818:Animals; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism; D002454:Cell Differentiation; D002462:Cell Membrane; D005677:G(M1) Ganglioside / Q000502:physiology*; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D009419:Nerve Tissue Proteins / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D009435:Synaptic Transmission
chemical_list: D006023:Glycoproteins; D009419:Nerve Tissue Proteins; D005677:G(M1) Ganglioside; D002118:Calcium
keywords: GM1 ganglioside; GPCR modulation; ion transport regulation; lipid rafts; neuritogenesis; neurodegenerative diseases; neurotrophic support