J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/07/395/15 $2.00
Volume 138, Number 2, July 28, 1997 395-409

KLP38B: A Mitotic Kinesin-related Protein That Binds PP1

Luke Alphey,^* Louise Parker,^* Gillian Hawcroft,^* Yiquan Guo, Kim Kaiser, and Gareth Morgan^*

^* School of Biological Sciences, University of Manchester, Manchester M13 9PT; and  Division of Molecular Genetics, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G11 6NU, United Kingdom

We have identified a new member of the kinesin superfamily in Drosophila, KLP38B (kinesin-like protein at 38B). KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP1 associate in vitro. This is the first demonstration of direct binding of a kinesin-related protein to a regulatory enzyme.

Though most closely related to the Unc-104 subfamily of kinesin-related proteins, KLP38B is expressed only in proliferating cells. KLP38B mutants show cell proliferation defects in many tissues. KLP38B is required for normal chromatin condensation as embryos from KLP38B mutant mothers have undercondensed chromatin at metaphase and anaphase. This is the first time that a kinesin-related protein has been shown to have such a role. Incomplete lethality of a strong KLP38B allele suggests partial redundancy with one or more additional kinesin-related proteins.

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