ArticleThe Journal of cell biology1988
Functional alterations in beta'-actin from a KB cell mutant resistant to cytochalasin B.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Cytochalasans and Their Impact on Actin Filament Remodeling.Biomolecules · 2023Review
- Article
- Proteomic analysis of proteins associated with cellular senescence by calorie restriction in mesenchymal stem cells.In vitro cellular & developmental biology. Animal · 2012Article
- Toxoplasma gondii rhoptry discharge correlates with activation of the early growth response 2 host cell transcription factor.Infection and immunity · 2008Article
- Gliding motility leads to active cellular invasion by Cryptosporidium parvum sporozoites.Infection and immunity · 2005Article
- How an actin network might cause fountain streaming and nuclear migration in the syncytial Drosophila embryo.The Journal of cell biology · 1994Article
- Direct proof that the primary site of action of cytochalasin on cell motility processes is actin.The Journal of cell biology · 1992Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We recently described the isolation of mutant KB cells (Cyt 1 cells) resistant to the cytotoxic effect of cytochalasin B (CB). This mutant carried an altered beta-actin; i.e., beta'-actin (Toyama, S., and S. Toyama. 1984. Cell. 37:609-614). In the present study, we have examined the functional properties of actin in Cyt 1 cells. Our results showed that increased resistance of Cyt 1 cells to CB was reflected in altered properties of beta'-actin itself. This was shown directly by two findings. First, the polymerization of beta'-actin was more resistant than that of beta- or gamma-actin to the multiple effects of CB. Second, beta'-actin bound less CB than beta- or gamma-actin. The functional alteration of beta'-actin in Cyt 1 cells was further supported by the observation that, although treatment of KB cells with CB increased the pool of unpolymerized actin, the same treatment did not affect the pool of unpolymerized actin in Cyt 1 cells, and that microfilaments of Cyt 1 cells were more resistant to the disrupting action of CB than those of KB cells. These results strongly suggest that the primary site of action of CB on cell motility processes is actin.
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