KLP38B: A Mitotic Kinesin-related Protein That Binds PP1
| Autor: | Gareth Morgan, Kim Kaiser, Luke Alphey, Gillian Hawcroft, Louise Parker, Yiquan Guo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Male
DNA Complementary Protein subunit Phosphatase Molecular Sequence Data Restriction Mapping Kinesins Mitosis macromolecular substances Biology Article Gene Expression Regulation Enzymologic 03 medical and health sciences 0302 clinical medicine Phosphoprotein Phosphatases Animals Drosophila Proteins Amino Acid Sequence RNA Messenger Cloning Molecular Metaphase 030304 developmental biology Anaphase 0303 health sciences Base Sequence Sequence Homology Amino Acid Cell Cycle Cell Biology Sequence Analysis DNA Chromatin Fertility Biochemistry Organ Specificity Mutation Kinesin Drosophila Female 030217 neurology & neurosurgery Drosophila Protein Cell Division |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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