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Papers In Press, published online ahead of print May 31, 2002
Molecular Virology Section, National Institutes of Allergy & Infectious Diseases, Bethesda, MD 20892-0460
Corresponding Author: kj7e{at}nih.gov
In eukaryotes, the mitotic spindle assembly checkpoint provides a monitor for the fidelity of chromosomal segregation. In this context, the mitotic arrest deficiency protein 2 (MAD2) censors chromosomal missegregation by monitoring microtubule attachment/tension, a role which requires its attachment to kinetochores. Studies in yeast have shown that binding of MAD1 to MAD2 is important for the latter’s checkpoint function. The interactions between human MAD1 (hsMAD1) and human MAD2 (hsMAD2) have, however, remained poorly characterized. Here, we report that two leucine zipper domains (amino acids 501-522 and 557-571) in hsMAD1 are required for its contact with hsMAD2. Interestingly, in several cancer cell lines, we noted the frequent presence of a coding single-nucleotide R to H polymorphism at codon 558 located within the second leucine zipper of hsMAD1. We found that hsMAD1H558 is less proficient than hsMAD1R558 in binding hsMAD2 and in enforcing mitotic arrest. We also document a first example of loss-of-heterozygosity (LOH) for a spindle checkpoint gene (at the hsMAD1 558 locus) in a human breast cancer. Based on our findings, it is possible that hsMAD1H558 could be an at-risk polymorphism which contributes to attenuated spindle checkpoint function in human cells.
J. Biol. Chem, 10.1074/jbc.M110666200
Submitted on November 6, 2001
Revised on April 17, 2002
Accepted on May 31, 2002
Characterization of regions in hsMAD1 needed for binding hsMAD2: a polymorphic change in an hsMAD1 leucine zipper affects MAD1-MAD2 interaction and spindle checkpoint function
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