Drosophila substrate adhesion molecule: sequence of laminin B1 chain reveals domains of homology with mouse.

TitleDrosophila substrate adhesion molecule: sequence of laminin B1 chain reveals domains of homology with mouse.
Publication TypeJournal Article
Year of Publication1988
AuthorsMontell DJ, Goodman CS
JournalCell
Volume53
Issue3
Pagination463-73
Date Published1988 May 06
ISSN0092-8674
KeywordsAmino Acid Sequence, Animals, Axons, Base Sequence, Cell Adhesion, Cell Movement, Cloning, Molecular, DNA, Drosophila, Gene Expression Regulation, Laminin, Mice, Molecular Sequence Data, Nucleic Acid Hybridization, Repetitive Sequences, Nucleic Acid, Sequence Homology, Nucleic Acid
Abstract

<p>Laminin, a substrate adhesion molecule in vertebrates, is a large glycoprotein complex in basement membranes that promotes cell adhesion, cell migration, and neurite outgrowth. Here we report on the cloning of the genes encoding the three subunits of Drosophila laminin. Sequence analysis of cDNA clones encoding the Drosophila B1 chain reveals a multidomain structure similar to that of its mouse homolog. The Drosophila sequence has only 25% amino acid identity with the mouse sequence in domains I, II, and IV. However, in one of the putative collagen-binding regions (domain VI) and the two cysteine-rich domains of EGF-like repeats (domains III and V), the amino acid identity between these two evolutionarily distant species jumps to 55%. Moreover, the number, length, and unique amino acid sequences of each of the 13 EGF-like repeats are highly conserved between Drosophila and mouse, suggesting that each may serve a unique function in protein-protein interactions.</p>

DOI10.1016/0092-8674(88)90166-3
Alternate JournalCell
PubMed ID3365769