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Cell Cycle, Cell Death, and Senescence

repp86: A Human Protein Associated in the Progression of Mitosis^1,2

¹ Department of Hematopathology and Lymph Node Registry, ² Department of Immunology and ³ 1st Department of Medicine, University of Kiel, Kiel, Germany;
⁴ Department of Cell Biochemistry and Clinical Neurobiology, University of Hamburg, Hamburg, Germany; and
⁵ Division of Molecular Immunology, Research Center Borstel, Germany

Requests for reprints: Hans-Juergen Heidebrecht, Department of Hematopathology, University of Kiel, Michaelisstr. 11, D-24105 Kiel, Germany. Phone: 49-431-597-3393; Fax: 49-431-597-3428. E-mail: hheidebrecht{at}path.uni-kiel.de

Human repp86 becomes detectable in the nucleoplasm of cycling cells at the G₁-S boundary, condenses at the centrosomes with the onset of mitosis, during which it progressively locates to the mitotic spindle and to the midbody, and vanishes at the completion of cytokinesis. The repp86 cDNA was cloned and sequenced. Full-length repp86 and its COOH-terminal domain cosediment with polymerized microtubules, linking repp86 to the family of microtubule-associated proteins. During prophase and metaphase, repp86 interacts on the mitotic spindle with the putative motor protein Hklp2. Thus, repp86 may function in targeting Hklp2 to the microtubule minus ends, its activity being regulated by phosphorylation of serine/threonine residues. Exogenous overexpression of repp86 provokes accumulation of cells in G₂-M phase and subsequent polyploidization, suggesting that excess repp86 may interfere with correct nuclear division.

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