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Analysis of biophysical and functional consequences of tropomyosin–fluorescent protein fusions
Author(s) -
Brooker Holly R.,
Geeves Michael A.,
Mulvihill Daniel P.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12346
Subject(s) - tropomyosin , actin , actin remodeling , microbiology and biotechnology , actin binding protein , fluorescence , biophysics , biology , labelling , gene isoform , chemistry , biochemistry , cell , actin cytoskeleton , cytoskeleton , gene , physics , quantum mechanics
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.