ArticleThe Journal of cell biology1996
DSK1, a novel kinesin-related protein from the diatom Cylindrotheca fusiformis that is involved in anaphase spindle elongation.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Origin and evolution of Kinesin-like calmodulin-binding protein.Plant physiology · 2005Article
- Kinesins in the Arabidopsis genome: a comparative analysis among eukaryotes.BMC genomics · 2001Article
- The polarity and dynamics of microtubule assembly in the budding yeast Saccharomyces cerevisiae.Nature cell biology · 2000Article
- Nuclear organization and chromosome segregation.The Plant cell · 1999Review
- Mitotic centromere-associated kinesin is important for anaphase chromosome segregation.The Journal of cell biology · 1998Article
- Anaphase in vitro.Proceedings of the National Academy of Sciences of the United States of America · 1996Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have identified an 80-kD protein that is involved in mitotic spindle elongation in the diatom Cylindrotheca fusiformis. DSK1 (Diatom Spindle Kinesin 1) was isolated using a peptide antibody raised against a conserved region in the motor domain of the kinesin superfamily. By sequence homology, DSK1 belongs to the central motor family of kinesin-related proteins. Immunoblots using an antibody raised against a non-conserved region of DSK1 show that DSK1 is greatly enriched in mitotic spindle preparations. Anti-DSK1 stains in diatom central spindle with a bias toward the midzone, and staining is retained in the spindle midzone during spindle elongation in vitro. Furthermore, preincubation with anti-DSK1 blocks function in an in vitro spindle elongation assay. This inhibition of spindle elongation can be rescued by preincubating concurrently with the fusion protein against which anti-DSK1 was raised. We conclude that DSK1 is involved in spindle elongation and is likely to be responsible for pushing hal-spindles apart in the spindle midzone.
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Registered trials
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