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© The Rockefeller University Press,
0021-9525/1999//191 $5.00
The Journal of Cell Biology, Volume 145, Number 1,
, 1999 191-201
Regular Articles |
wing blister, A New Drosophila Laminin 
Chain Required for Cell Adhesion and Migration during Embryonic and Imaginal Development
Department of Cell and Molecular Biology, Lund University, S-22100 Lund, Sweden; and Department of Biology, University of Rochester, Rochester, New York 14627
We report the molecular and functional characterization of a new
chain of laminin in Drosophila. The new laminin chain appears to be the Drosophila counterpart of both vertebrate 2 (also called merosin) and 1 chains, with a slightly higher degree of homology to 2, suggesting that this chain is an ancestral version of both 1 and 2 chains. During embryogenesis, the protein is associated with basement membranes of the digestive system and muscle attachment sites, and during larval stage it is found in a specific pattern in wing and eye discs. The gene is assigned to a locus called wing blister (wb), which is essential for embryonic viability. Embryonic phenotypes include twisted germbands and fewer pericardial cells, resulting in gaps in the presumptive heart and tracheal trunks, and myotubes detached from their target muscle attachment sites. Most phenotypes are in common with those observed in Drosophila laminin 3, 5 mutant embryos and many are in common with those observed in integrin mutations. Adult phenotypes show blisters in the wings in viable allelic combinations, similar to phenotypes observed in integrin genes. Mutation analysis in the eye demonstrates a function in rhabdomere organization. In summary, this new laminin chain is essential for embryonic viability and is involved in processes requiring cell migration and cell adhesion.
Key Words: Drosophila • wing blister • laminin • extracellular matrix • development
Abbreviations used in this paper: BM, basement membrane; ECM, extracellular matrix; wb, wing blister.
Sequence data reported in this paper appears in GenBank/EMBL/DDBJ under the accession number AF 135118.
D. Martin and S. Zusman contributed equally to this work.
S. Zusman and X. Li's present address is Department of Functional Genomics, Novartis Pharmaceuticals, Life Sciences Building, 556 Moris Avenue, Summit, NJ 07901-1398. E.L. Williams' present address is Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77096.
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