Kinesins are microtubule (MT)-based motors involved in various cellular functions including intracellular transport of vesicles and organelles, and dynamics of chromosomes during cell division. The fission yeast Schizosaccharomyces pombe expresses nine kinesin-like proteins (klps). Klp8 is one of them and has not been characterized yet though it has been reported to localize at the division site. Here, we studied function and localization of Klp8 in S. pombe cells. The gene klp8+ was not essential for both viability and cytoskeletal organization. Klp8-YFP was concentrated as medial cortical dots during interphase, and organized into a ring at the division site during mitosis. The Klp8 ring seemed to be localized in the space between the actomyosin contractile ring and the plasma membrane. The Klp8 ring shrank as cytokinesis proceeded. In klp8-deleted (Δ) cells, the speed of spindle elongation during anaphase B was slowed down. Overproduction of Klp8 caused bent or elongated cells, in which MTs were abnormally elongated and less dynamic than those in normal cells. Deletion of klp8+ gene suppressed the delay in mitotic entry in blt1Δ cells. These results suggest that Klp8 is involved in mitosis and cell morphology through MT stabilization.
Keywords: contractile ring; fission yeast; kinesin; microtubule; mitosis.
© 2019 Wiley Periodicals, Inc.