Ganglioside mediate the interaction between Nogo receptor 1 and LINGO-1

► GT1b influences the interaction of NgR1 and LINGO-1. ► Stalk of NgR1 is important for this interaction. ► Sialic acid moiety of GT1b is necessary and sufficient for this interaction. ► The NgR1/LINGO-1/GT1b complex retains the ability to bind Nogo-A and p75 simultaneously. Upon spinal cord injury,...

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Published in:Biochemical and biophysical research communications 2011-09, Vol.413 (1), p.92-97
Main Authors: Saha, Nayanendu, Kolev, Momchil V., Semavina, Mariya, Himanen, Juha, Nikolov, Dimitar B.
Format: Article
Language:English
Subjects:
Cell-Free System - metabolism
Ganglioside
Gangliosides - metabolism
GPI-Linked Proteins - genetics
GPI-Linked Proteins - metabolism
HEK293 Cells
Humans
LINGO-1
Membrane Proteins - metabolism
Myelin Proteins - genetics
Myelin Proteins - metabolism
N-Acetylneuraminic Acid - chemistry
N-Acetylneuraminic Acid - metabolism
Nerve Tissue Proteins - metabolism
Nogo Proteins
Nogo receptor
Nogo Receptor 1
Nogo-A
p75
Protein Structure, Tertiary
Receptor, Nerve Growth Factor - metabolism
Receptors, Cell Surface - genetics
Receptors, Cell Surface - metabolism
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Summary:► GT1b influences the interaction of NgR1 and LINGO-1. ► Stalk of NgR1 is important for this interaction. ► Sialic acid moiety of GT1b is necessary and sufficient for this interaction. ► The NgR1/LINGO-1/GT1b complex retains the ability to bind Nogo-A and p75 simultaneously. Upon spinal cord injury, the myelin inhibitors, including the myelin-associated glycoprotein (MAG), Nogo-A and the oligodendrocyte myelin glycoprotein (OMgp), bind to and signal via a single neuronal receptor/co-receptor complex comprising of Nogo receptor 1(NgR1)/LINGO-1 and p75 or TROY, impeding regeneration of injured axons. We employed a cell-free system to study the binding of NgR1 to its co-receptors and the myelin inhibitor Nogo-A, and show that gangliosides mediate the interaction of NgR1 with LINGO-1. Solid phase binding assays demonstrate that the sialic acid moieties of gangliosides and the stalk of NgR1 are the principal determinants of these molecular interactions. Moreover, the tripartite complex comprising of NgR1, LINGO-1 and ganglioside exhibits stronger binding to Nogo-A (Nogo-54) in the presence of p75, suggesting the gangliosides modulate the myelin inhibitor-receptor signaling.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2011.08.060