Neurexins, Neuroligins and LRRTMs: synaptic adhesion getting fishy

作者: Gavin J. Wright , Philip Washbourne

DOI: 10.1111/J.1471-4159.2010.07141.X

关键词:

摘要: Recent studies have identified the leucine rich repeat protein LRRTM2 as a post-synaptic ligand of Neurexins. Neurexins also bind adhesion molecules, Neuroligins. All three families genes been implicated in etiologies neurodevelopmental disorders, specifically autism spectrum disorders and schizophrenia. Does binding promiscuity now suggest complex cooperativity or redundancy at synapse? While recent primary neuronal cultures systematic extracellular interaction screens summative effects these systems, we propose that studying interactions developing zebrafish embryo larvae may shed more light on their functions during synaptogenesis vivo. These gene recently extensively characterized zebrafish, demonstrating high sequence conservation with human genes. The simpler circuitry together characterization expression patterns down to single, identifiable neurons ability knock-down over-express multiple rapid way lend themselves dissecting pathways. Furthermore, capability performing high-throughput drug suggests small vertebrates prove extremely useful identifying pharmacological approaches treating disorders.

参考文章(138)
S. de la Escalera, E. O. Bockamp, F. Moya, M. Piovant, F. Jiménez, Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases. The EMBO Journal. ,vol. 9, pp. 3593- 3601 ,(1990) , 10.1002/J.1460-2075.1990.TB07570.X
P.F. Olson, L.I. Fessler, R.E. Nelson, R.E. Sterne, A.G. Campbell, J.H. Fessler, Glutactin, a novel Drosophila basement membrane‐related glycoprotein with sequence similarity to serine esterases. The EMBO Journal. ,vol. 9, pp. 1219- 1227 ,(1990) , 10.1002/J.1460-2075.1990.TB08229.X
Thomas Biederer, Thomas C. Südhof, CASK and protein 4.1 support F-actin nucleation on neurexins. Journal of Biological Chemistry. ,vol. 276, pp. 47869- 47876 ,(2001) , 10.1074/JBC.M105287200
Benjamin Feldman, Michael A. Gates, Elizabeth S. Egan, Scott T. Dougan, Gabriela Rennebeck, Howard I. Sirotkin, Alexander F. Schier, William S. Talbot, Zebrafish organizer development and germ-layer formation require nodal-related signals Nature. ,vol. 395, pp. 181- 185 ,(1998) , 10.1038/26013
Xiaolin L. He, J.Fernando Bazan, Gerry McDermott, Jong Bae Park, Kevin Wang, Marc Tessier-Lavigne, Zhigang He, K.Christopher Garcia, Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition. Neuron. ,vol. 38, pp. 177- 185 ,(2003) , 10.1016/S0896-6273(03)00232-0
Y. A. Ushkaryov, T. C. Sudhof, S. Afendis, Clive A. Slaughter, C. Moomaw, Y. Hata, K. Ichtchenko, Conserved domain structure of beta-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins. Journal of Biological Chemistry. ,vol. 269, pp. 11987- 11992 ,(1994) , 10.1016/S0021-9258(17)32671-6
Markus Missler, Weiqi Zhang, Astrid Rohlmann, Gunnar Kattenstroth, Robert E. Hammer, Kurt Gottmann, Thomas C. Südhof, Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis. Nature. ,vol. 423, pp. 939- 948 ,(2003) , 10.1038/NATURE01755
Randall T. Peterson, Mark C. Fishman, Discovery and use of small molecules for probing biological processes in zebrafish. Methods in Cell Biology. ,vol. 76, pp. 569- 591 ,(2004) , 10.1016/S0091-679X(04)76026-4
I Correas, D W Speicher, V T Marchesi, Structure of the spectrin-actin binding site of erythrocyte protein 4.1. Journal of Biological Chemistry. ,vol. 261, pp. 13362- 13366 ,(1986) , 10.1016/S0021-9258(18)69313-5