Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor α convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2β Journal Article
| Authors: | Nelson, K. K.; Schlöndorff, J.; Blobel, C. P. |
| Article Title: | Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor α convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2β |
| Abstract: | Metalloprotease-disintegrins are a family of transmembrane glycoproteins that have a role in fertilization, sperm migration, myoblast fusion, neural development and ectodomain shedding. In the present study we used the yeast two-hybrid system to search for proteins that interact with the cytoplasmic domain of two metalloprotease-disintegrins, tumour necrosis factor α convertase (TACE; ADAM17) and MDC9 (ADAM9; meltrin γ). We have identified mitotic arrest deficient 2 (MAD2) as a binding partner of the TACE cytoplasmic domain, and a novel MAD2-related protein, MAD2β, as a binding partner of the MDC9 cytoplasmic domain. MAD2β has 23% sequence identity with MAD2, which is a component of the spindle assembly (or mitotic) checkpoint mechanism. Northern blot analysis of human tissues indicates that MAD2β mRNA is expressed ubiquitously. The interaction of the TACE and MDC9 cytoplasmic domains with their binding partners has been confirmed biochemically. The independent identification of MAD2 and MAD2β as potential interacting partners of distinct metalloprotease-disintegrins raises the possibility of a link between metalloprotease-disintegrins and the cell cycle, or of functions for MAD2 and MAD2β that are not related to cell cycle control. |
| Keywords: | protein expression; sequence analysis; dna-binding proteins; nonhuman; animal cell; animals; cell cycle proteins; cell cycle; smad2 protein; protein protein interaction; membrane proteins; transfection; cos cells; animalia; nuclear proteins; cloning, molecular; amino acid sequence; molecular sequence data; sequence homology, amino acid; tumor necrosis factor alpha; tumor necrosis factor-alpha; messenger rna; saccharomyces cerevisiae; sequence alignment; carrier proteins; recombinant proteins; cytoplasm; calcium-binding proteins; trans-activators; yeast; saccharomyces cerevisiae proteins; monkey; glycoprotein; fibroblast culture; metalloproteinase; adam proteins; myoblast; northern blotting; fungal proteins; mitosis inhibition; mad2; fertilization; disintegrin; mdc9; disintegrins; metalloendopeptidases; tace; humans; priority journal; article; adams; yeast two-hybrid screen; spermatozoon migration |
| Journal Title: | Biochemical Journal |
| Volume: | 343 |
| Issue: | 3 |
| ISSN: | 0264-6021 |
| Publisher: | Portland Press Ltd |
| Date Published: | 1999-11-01 |
| Start Page: | 673 |
| End Page: | 680 |
| Language: | English |
| DOI: | 10.1042/0264-6021:3430673 |
| PUBMED: | 10527948 |
| PROVIDER: | scopus |
| PMCID: | PMC1220601 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
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