Fasciclin III: A novel homophilic adhesion molecule in Drosophila

Peter M. Snow, Allan J. Bieber, Corey S. Goodman

Research output: Contribution to journalArticlepeer-review

146 Scopus citations


Drosophila fasciclin III is an integral membrane glycoprotein that is expressed on a subset of neurons and fasciculating axons in the developing CNS, as well as in several other tissues during development. Here we report on the isolation of a full-length cDNA encoding an 80 kd form of fasciclin III. We have used this cDNA, under heat shock control, to transfect the relatively nonadhesive Drosophila S2 cell line. Examination of these transfected cells indicates that fasciclin III is capable of mediating adhesion in a homophilic, Ca2+-independent manner. Sequence analysis reveals that fasciclin III encodes a transmembrane protein with no significant homology to any known protein, including the previously characterized families of vertebrate cell adhesion molecules. The distribution of this adhesion molecule on subsets of fasciculating axons and growth cones during Drosophila development suggests that fasciclin III plays a role in growth cone guidance.

Original languageEnglish (US)
Pages (from-to)313-323
Number of pages11
Issue number2
StatePublished - Oct 20 1989

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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