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Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases.
Author(s) -
Escalera S.,
Bockamp E. O.,
Moya F.,
Piovant M.,
Jiménez F.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb07570.x
Subject(s) - biology , cloning (programming) , gene , genetics , drosophila (subgenus) , drosophila melanogaster , transmembrane protein , molecular cloning , peptide sequence , receptor , computer science , programming language
Monoclonal antibodies have served to characterize neurotactin, a novel Drosophila protein for which a role in cell adhesion is postulated. Neurotactin is a transmembrane protein, as indicated by epitope mapping and amino acid sequence. Similarly to other cell adhesion molecules, neurotactin accumulates in parts of the membrane where neurotactin‐expressing cells contact each other. The protein is only detected during cell proliferation and differentiation, and it is found mainly in neural tissue and also in mesoderm and imaginal discs. Neurotactin has a large cytoplasmic domain rich in charged residues and an extracellular domain similar to cholinesterase that lacks the active site serine required for esterase activity. The extracellular domain also contains three copies of the tripeptide leucine‐arginine‐glutamate, a motif that forms the primary sequence of the adhesive site of vertebrate s‐laminin.