Leucine‐rich glioma inactivated 1 ( LGI1 ) is a ganglioside‐binding protein
Abstract
In Lgi1 −/− mice, increased neuronal excitability is accompanied by a marked decrease in Kv1 channels, but the mechanism linking LGI1 loss to reduced ion channel expression remains unknown. We show that LGI1 contains multiple conserved canonical ganglioside‐binding domains (GBDs) and that GT1b copurifies with LGI1 antibodies from native rat brain extracts. Recombinant LGI1 bound ganglioside‐containing liposomes, and the ganglioside‐binding capacity of surface‐exposed GBD peptide sequences was confirmed experimentally. These findings suggest LGI1 interacts with gangliosides and may help organize lipid membrane platforms that accommodate functional protein complexes. We hypothesize that loss of LGI1 destabilizes these platforms, contributing to the reduced ion channel expression observed in Lgi1 −/− mice.
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BibTeX
@article{debreux2026leucinerich,
title = {{Leucine‐rich glioma inactivated 1 ( LGI1 ) is a ganglioside‐binding protein}},
author = {Kévin Debreux and Christian Lévêque and Fodil Azzaz and Marion Sangiardi and Sarosh Irani and Michael Seagar and Jacques Fantini and Oussama El Far},
journal = {FEBS Letters},
year = {2026},
month = sep,
doi = {10.1002/1873-3468.70465},
url = {https://inserm.hal.science/inserm-05758508v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Leucine‐rich glioma inactivated 1 ( LGI1 ) is a ganglioside‐binding protein
AU - Kévin Debreux
AU - Christian Lévêque
AU - Fodil Azzaz
AU - Marion Sangiardi
AU - Sarosh Irani
AU - Michael Seagar
AU - Jacques Fantini
AU - Oussama El Far
PY - 2026
DA - 2026/09/15
JO - FEBS Letters
DO - 10.1002/1873-3468.70465
UR - https://inserm.hal.science/inserm-05758508v1
AB - In Lgi1 −/− mice, increased neuronal excitability is accompanied by a marked decrease in Kv1 channels, but the mechanism linking LGI1 loss to reduced ion channel expression remains unknown. We show that LGI1 contains multiple conserved canonical ganglioside‐binding domains (GBDs) and that GT1b copurifies with LGI1 antibodies from native rat brain extracts. Recombinant LGI1 bound ganglioside‐containing liposomes, and the ganglioside‐binding capacity of surface‐exposed GBD peptide sequences was confirmed experimentally. These findings suggest LGI1 interacts with gangliosides and may help organize lipid membrane platforms that accommodate functional protein complexes. We hypothesize that loss of LGI1 destabilizes these platforms, contributing to the reduced ion channel expression observed in Lgi1 −/− mice.
SN - 0014-5793
SN - 1873-3468
ER -