By a News Reporter-Staff News Editor at Science Letter -- Current study results on Cell Science have been published. According to news reporting originating from Beer Sheva, Israel, by NewsRx correspondents, research stated, "In this study, we examined the anaphase functions of the S. cerevisiae kinesin-5 homolog Kip1. We show that Kip1 is attached to the mitotic spindle midzone during late anaphase."
Our news editors obtained a quote from the research from the Ben-Gurion University of the Negev, "This attachment is essential to stabilize interpolar microtubule (iMTs) plus-ends. By detailed examination of iMT dynamics we show that at the end of anaphase, iMTs depolymerize in two stages: during the first stage, one pair of anti-parallel iMTs depolymerizes at a velocity of 7.7 mu m/minute; during the second stage, similar to 90 seconds later, the remaining pair of iMTs depolymerizes at a slower velocity of 5.4 mu m/minute. We show that upon the second depolymerization stage, which coincides with spindle breakdown, Kip1 follows the plus-ends of depolymerizing iMTs and translocates toward the spindle poles. This movement is independent of mitotic microtubule motor proteins or the major plus-end binding or tracking proteins. In addition, we show that Kip1 processively tracks the plus-ends of growing and shrinking MTs, both inside and outside the nucleus. The plus-end tracking activity of Kip1 requires its catalytic motor function, because a rigor mutant of Kip1 does not exhibit this activity. Finally, we show that Kip1 is a bi-directional motor: in vitro, at high ionic strength conditions, single Kip1 molecules move processively in the minus-end direction of the MTs, whereas in a multi-motor gliding assay, Kip1 is plus-end directed."
According to the news editors, the research concluded: "The bi-directionality and plus-end tracking activity of Kip1, properties revealed here for the first time, allow Kip1 to perform its multiple functions in mitotic spindle dynamics and to partition the 2-micron plasmid."
For more information on this research see: Kinesin-5 Kip1 is a bi-directional motor that stabilizes microtubules and tracks their plus-ends in vivo. Journal of Cell Science, 2013;126(18):4147-4159. Journal of Cell Science can be contacted at: Company Of Biologists Ltd, Bidder Building Cambridge Commercial Park Cowley Rd, Cambridge CB4 4DL, Cambs, England (see also Cell Science).
The news editors report that additional information may be obtained by contacting V. Fridman, Ben Gurion University of the Negev, Ilse Katz Inst Nanoscale Sci & Technol, IL-84105 Beer Sheva, Israel. Additional authors for this research include A. Gerson-Gurwitz, O. Shapira, N. Movshovich, S. Lakamper, C.F. Schmidt and L. Gheber.
Keywords for this news article include: Asia, Israel, Beer Sheva, Cell Science
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