Laminin-dependent integrin clustering with tyrosine-phosphorylated molecules in a Drosophila neuronal cell line

Neurosci Lett. 1998 Mar 20;244(3):149-52. doi: 10.1016/s0304-3940(98)00145-1.


To gain more insight into the molecular and cellular aspects of basement membranes during Drosophila morphogenesis, especially in neural development, we carried out cell biological screening to establish a cell culture system in which Drosophila cell-matrix interaction could be reconstituted. The screening showed that a Drosophila neuronal cell line, BG2-c6, established from the third-instar larval central nervous system, had a strong adhesion activity when purified Drosophila laminin was used as a substrate. Outgrowth of axon-like structures was stimulated on laminin. Histochemical analysis revealed clusters of integrin together with phosphotyrosine and alpha-actinin. These data indicate that the Drosophila integrin cascade triggered by the interaction between BG2-c6 and laminin was initiated at the integrin cluster with tyrosine-phosphorylated proteins, similar to the observations in vertebrate cells.

MeSH terms

  • Animals
  • Cells, Cultured
  • Drosophila / cytology
  • Drosophila / embryology*
  • Histocytochemistry
  • Insect Proteins / metabolism
  • Integrins / metabolism*
  • Laminin / physiology*
  • Neurons / chemistry
  • Neurons / metabolism*
  • Phosphorylation
  • Signal Transduction
  • Tyrosine / metabolism*


  • Insect Proteins
  • Integrins
  • Laminin
  • Tyrosine