Biochem. J. (1999) 343
(673–680) (Printed in Great Britain)
Evidence for an interaction of the metalloprotease–disintegrin tumour necrosis factor a convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease–disintegrin MDC9 with a novel MAD2-related protein, MAD2b
Karen K. NELSON*1, Johannes SCHLÖNDORFF*†1 and Carl P. BLOBEL*2
*Cellular Biochemistry and Biophysics Program, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, U.S.A., and †Tri-Institutional (Cornell/Rockefeller University/Memorial Sloan-Kettering Cancer Center) MD/PhD Training Program, New York, NY 10021, U.S.A.
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 a convertase (TACE; ADAM17) and MDC9 (ADAM9; meltrin g). We have identified mitotic arrest deficient 2 (MAD2) as a binding partner of the TACE cytoplasmic domain, and a novel MAD2-related protein, MAD2b, as a binding partner of the MDC9 cytoplasmic domain. MAD2b 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 MAD2b 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 MAD2b 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 MAD2b that are not related to cell cycle control.
Abbreviations used: APC, anaphase-promoting complex; FLAG, Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys; GST, glutathione S-transferase; MAD2, mitotic arrest deficient 2; TACE, tumour necrosis factor
a convertase.
1 These authors contributed equally to this work.
2 To whom correspondence should be addressed (e-mail c-blobel@ski.mskcc.org).
Key words: ADAMs, MAD2, MDC9, TACE, yeast two-hybrid screen.
Received 28 April 1999/12 July 1999; accepted 31 August 1999
The Biochemical Society, London © 1999
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