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Science 21 July 1995:
Vol. 269. no. 5222, pp. 413 - 416
DOI: 10.1126/science.7618109
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Articles

Science, Vol 269, Issue 5222, 413-416
Copyright © 1995 by American Association for the Advancement of Science

articles

A synaptic localization domain in the synaptic cleft protein laminin beta 2 (s-laminin)

PT Martin, AJ Ettinger, and Sanes JR

Department of Anatomy and Neurobiology, Washington University School of Medicine, St.Louis, MO 63110, USA.

The basal lamina that ensheaths skeletal muscle fibers traverses the synaptic cleft at the neuromuscular junction. Synaptic and extrasynaptic portions of the basal lamina contain different laminin beta chains: beta 2 (or s) at synapses and beta 1 (or B1) extrasynaptically. Laminin beta 2 is also confined to synapselike patches on myotube surfaces in vitro, whereas beta 1 is present throughout the extracellular matrix. This differential localization of laminin beta chains was analyzed by expression of chimeric beta 1-beta 2 molecules in cultured mouse myotubes. A 16-amino acid carboxyl-terminal sequence in beta 2 was necessary for synaptic localization, and an amino-terminal domain in beta 1 promoted association with extracellular fibrils. The synaptic targeting sequence of beta 2 contains a site previously shown to be adhesive for motor neurons.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Functional analysis of neurotransmission at {beta}2-laminin deficient terminals.
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Glomerular laminin isoform transitions: errors in metanephric culture are corrected by grafting.
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Binding of Injected Laminin to Developing Kidney Glomerular Mesangial Matrices and Basement Membranes In Vivo.
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Laminin-induced Acetylcholine Receptor Clustering: An Alternative Pathway.
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Agrin Binds to the Nerve-Muscle Basal Lamina via Laminin.
A. J. Denzer, R. Brandenberger, M. Gesemann, M. Chiquet, and M. A. Ruegg (1997)
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Laminin beta 2 (S-laminin): a new player at the synapse.
Z. Hall (1995)
Science 269, 362-363
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