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.
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, vulva, and mature sperm is consistent with a putative role in somatic and gamete cell fusions.
Podbilewicz
B
B
Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
D051722:ADAM Proteins; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D017173:Caenorhabditis elegans / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins; D002874:Chromosome Mapping; D018076:DNA, Complementary; D019483:Disintegrins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000072196:Fertilins; D015801:Helminth Proteins / Q000235:genetics* / Q000378:metabolism; D008297:Male; D008562:Membrane Glycoproteins / Q000737:chemistry; D008666:Metalloendopeptidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D012333:RNA, Messenger; D017386:Sequence Homology, Amino Acid; D013094:Spermatozoa / Q000378:metabolism*
D029742:Caenorhabditis elegans Proteins; D018076:DNA, Complementary; D019483:Disintegrins; D015801:Helminth Proteins; D008562:Membrane Glycoproteins; D012333:RNA, Messenger; C104620:UNC-71 protein, C elegans; D051722:ADAM Proteins; D000072196:Fertilins; D008666:Metalloendopeptidases