Neuroligin 1 Induces Blood Vessel Maturation by Cooperating with the α6 Integrin
Abstract
The synaptic protein Neuroligin 1 (NLGN1), a cell adhesion molecule, is critical for the formation and consolidation of synaptic connectivity and is involved in vascular development. The mechanism through which NLGN1 acts, especially in vascular cells, is unknown. Here, we aimed at deepening our knowledge on the cellular activities and molecular pathways exploited by endothelial NLGN1 both in vitro and in vivo. We analyzed the phenotypic consequences of NLGN1 expression modulation in endothelial cells through in vitro angiogenesis assays and the mouse postnatal retinal angiogenesis model. We demonstrate that NLGN1, whereas not affecting endothelial cell proliferation or migration, modulates cell adhesion to the vessel stabilizing protein laminin through cooperation with the α6 integrin, a specific laminin receptor. Finally, we show that in vivo, NLGN1 and α6 integrin preferentially colocalize in the mature retinal vessels, whereas NLGN1 deletion causes an aberrant VE-cadherin, laminin and α6 integrin distribution in vessels, along with significant structural defects in the vascular tree.
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BibTeX
@article{samarelli2026neuroligin,
title = {{Neuroligin 1 Induces Blood Vessel Maturation by Cooperating with the α6 Integrin}},
author = {Anna Valeria Samarelli and Elena Riccitelli and Laura Bizzozero and Tatiana Nunes Silveira and Giorgio Seano and Margherita Pergolizzi and Grazia Vitagliano and Ilaria Cascone and Gilles Carpentier and Alessia Bottos and Luca Primo and Federico Bussolino and Marco Arese},
journal = {Journal of Biological Chemistry},
year = {2026},
month = oct,
doi = {10.1074/jbc.m113.530972},
url = {https://hal.science/hal-05801811v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - Neuroligin 1 Induces Blood Vessel Maturation by Cooperating with the α6 Integrin
AU - Anna Valeria Samarelli
AU - Elena Riccitelli
AU - Laura Bizzozero
AU - Tatiana Nunes Silveira
AU - Giorgio Seano
AU - Margherita Pergolizzi
AU - Grazia Vitagliano
AU - Ilaria Cascone
AU - Gilles Carpentier
AU - Alessia Bottos
AU - Luca Primo
AU - Federico Bussolino
AU - Marco Arese
PY - 2026
DA - 2026/10/15
JO - Journal of Biological Chemistry
DO - 10.1074/jbc.m113.530972
UR - https://hal.science/hal-05801811v1
AB - The synaptic protein Neuroligin 1 (NLGN1), a cell adhesion molecule, is critical for the formation and consolidation of synaptic connectivity and is involved in vascular development. The mechanism through which NLGN1 acts, especially in vascular cells, is unknown. Here, we aimed at deepening our knowledge on the cellular activities and molecular pathways exploited by endothelial NLGN1 both in vitro and in vivo. We analyzed the phenotypic consequences of NLGN1 expression modulation in endothelial cells through in vitro angiogenesis assays and the mouse postnatal retinal angiogenesis model. We demonstrate that NLGN1, whereas not affecting endothelial cell proliferation or migration, modulates cell adhesion to the vessel stabilizing protein laminin through cooperation with the α6 integrin, a specific laminin receptor. Finally, we show that in vivo, NLGN1 and α6 integrin preferentially colocalize in the mature retinal vessels, whereas NLGN1 deletion causes an aberrant VE-cadherin, laminin and α6 integrin distribution in vessels, along with significant structural defects in the vascular tree.
SN - 0021-9258
SN - 1083-351X
ER -