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J. Cell Biol.,
Volume 143, Number 7, December 28, 1998 1763-1774
* Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland, United Kingdom; and The inner centromere protein (INCENP)
has a modular organization, with domains required for
chromosomal and cytoskeletal functions concentrated
near the amino and carboxyl termini, respectively. In this study we have identified an autonomous centromere- and midbody-targeting module in the amino-terminal 68 amino acids of INCENP. Within this module, we have identified two evolutionarily conserved
amino acid sequence motifs: a 13-amino acid motif that is required for targeting to centromeres and transfer to
the spindle, and an 11-amino acid motif that is required
for transfer to the spindle by molecules that have targeted previously to the centromere. To begin to understand the mechanisms of INCENP function in mitosis, we have performed a yeast two-hybrid screen for interacting proteins. These and subsequent in vitro binding
experiments identify a physical interaction between INCENP and heterochromatin protein HP1Hs Department of Cell Biology and Anatomy, Johns Hopkins School of Medicine, Baltimore, Maryland 21218
. Surprisingly, this interaction does not appear to be involved in
targeting INCENP to the centromeric heterochromatin, but may instead have a role in its transfer from the
chromosomes to the anaphase spindle.
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