Collagens at the vertebrate neuromuscular junction, from structure to pathologies

Neurosci Lett. 2020 Sep 14:735:135155. doi: 10.1016/j.neulet.2020.135155. Epub 2020 Jun 10.


The extracellular matrix at the neuromuscular junction is built upon components secreted by the motoneuron, the muscle cell and terminal Schwann cells, the cells constituting this specific synapse. This compartment contains glycoproteins, proteoglycans and collagens that form a dense and specialized layer, the synaptic basal lamina. A number of these molecules are known to play a crucial role in anterograde and retrograde signalings that are active in neuromuscular junction formation, maintenance and function. Here, we focus on the isoforms of collagens which are enriched at the synapse. We summarize what we know of their structure, their function and their interactions with transmembrane receptors and other components of the synaptic basal lamina. A number of neuromuscular diseases, congenital myastenic syndromes and myasthenia gravis are caused by human mutations and autoantibodies against these proteins. Analysis of these diseases and of the specific collagen knock-out mice highlights the roles of some of these collagens in promoting a functional synapse.

Keywords: Collagens; Congenital myasthenic syndromes; Integrins; Junction; Myasthenia gravis; Neuromuscular; Perlecan.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Collagen*
  • Extracellular Matrix
  • Humans
  • Neuromuscular Junction*


  • Collagen