PMID: 8970152Dec 1, 1996Paper

ADM-1, a protein with metalloprotease- and disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in Caenorhabditis elegans

Molecular Biology of the Cell
B Podbilewicz

Abstract

A search was carried out for homologues of possible fusogenic proteins to study their function in a genetically tractable animal. The isolation, molecular, and cellular characterization of the Caenorhabditis elegans adm-1 gene (a disintegrin and metalloprotease domain) are described. A glycoprotein analogous to viral fusion proteins has been identified on the surface of guinea pig sperm (PH-30/fertilin) and is implicated in sperm-egg fusion. adm-1 is the first reported invertebrate gene related to PH-30 and a family of proteins containing snake venom disintegrin- and metalloprotease-like domains. ADM-1 shows a domain organization identical to PH-30. It contains prepro, metalloprotease, disintegrin, cysteine rich with putative fusion peptide, epidermal growth factor-like repeat, transmembrane, and cytoplasmic domains. Antibodies which recognize ADM-1 protein in immunoblots were generated. Using immunofluorescence and in situ hybridization, the products of adm-1 have been detected in specific cells during different stages of development. The localization of ADM-1 to the plasma membrane of embryonic cells and to the sheath cells of sensory organs suggests a function in cell adhesion. ADM-1 expression in the hypodermis, pharynx, vu...Continue Reading

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Citations

Jan 6, 2004·Nature Cell Biology·Benjamin Podbilewicz
Oct 22, 2008·Seminars in Cell & Developmental Biology·Dominique AlfandariHélène Cousin
Sep 3, 2002·Mechanisms of Development·Matthew Rise, Robert D Burke
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Mar 7, 2002·Developmental Cell·William A MohlerBenjamin Podbilewicz
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Jun 1, 1997·Trends in Cell Biology·D BiglerJ M White

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