Key result
Tropomyosin-fluorescent fusions decorate actin but are nonfunctional or perturb actin nucleation and cell cycle timings.
Why the study?
Different isoforms of tropomyosin regulate actin polymer dynamics and fluorescent labelling strategies for tropomyosin may affect its function and cellular processes.
Tropomyosin-fluorescent fusions can perturb actin regulation and cell cycle timings, indicating that their physiological relevance should be carefully evaluated.
Labelling strategies for tropomyosin isoforms require validation; extends actin subpopulation tools but leaves open cardiovascular applications.
The dynamic nature of actin polymers is modulated to facilitate a diverse range of cellular processes. These dynamic properties are determined by different isoforms of tropomyosin which are recruited to distinct subpopulations of actin polymers to differentially regulate their functional properties. This makes tropomyosin an attractive target for labelling discrete actin populations. We have assessed the effect of different fluorescent labelling strategies for this protein. Although tropomyosin-fluorescent fusions decorate actin in vivo, they are either nonfunctional or perturb regulation of actin nucleation and cell cycle timings. Thus, conclusions and physiological relevance should be carefully evaluated when using tropomyosin fusions.
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Brooker et al. (2016) studied this question. Tropomyosin-fluorescent protein fusions was evaluated on Regulation of actin nucleation and cell cycle timings. Tropomyosin-fluorescent fusions decorate actin in vivo but are either nonfunctional or perturb regulation of actin nucleation and cell cycle timings.
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