| Directionality of individual kinesin-5 Cin8 motors is modulated by loop 8, ionic strength and microtubule geometry. | |
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MedLine Citation:
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PMID: 22101328 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Kinesin-5 motors fulfil essential roles in mitotic spindle morphogenesis and dynamics as slow, processive microtubule (MT) plus-end directed motors. The Saccharomyces cerevisiae kinesin-5 Cin8 was found, surprisingly, to switch directionality. Here, we have examined directionality using single-molecule fluorescence motility assays and live-cell microscopy. On spindles, Cin8 motors mostly moved slowly (∼25 nm/s) towards the midzone, but occasionally also faster (∼55 nm/s) towards the spindle poles. In vitro, individual Cin8 motors could be switched by ionic conditions from rapid (380 nm/s) and processive minus-end to slow plus-end motion on single MTs. At high ionic strength, Cin8 motors rapidly alternated directionalities between antiparallel MTs, while driving steady plus-end relative sliding. Between parallel MTs, plus-end motion was only occasionally observed. Deletion of the uniquely large insert in loop 8 of Cin8 induced bias towards minus-end motility and affected the ionic strength-dependent directional switching of Cin8 in vitro. The deletion mutant cells exhibited reduced midzone-directed motility and efficiency to support spindle elongation, indicating the importance of directionality control for the anaphase function of Cin8. |
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Authors:
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Adina Gerson-Gurwitz; Christina Thiede; Natalia Movshovich; Vladimir Fridman; Maria Podolskaya; Tsafi Danieli; Stefan Lakämper; Dieter R Klopfenstein; Christoph F Schmidt; Larisa Gheber |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-18 |
Journal Detail:
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Title: The EMBO journal Volume: - ISSN: 1460-2075 ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-21 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8208664 Medline TA: EMBO J Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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