Analysis of biophysical and functional consequences of Tropomyosin - fluorescent protein fusions.

Brooker, H and Geeves, Michael A. and Mulvihill, Daniel P. (2016) Analysis of biophysical and functional consequences of Tropomyosin - fluorescent protein fusions. FEBS letters, . pp. 3111-3121. ISSN 1873-3468. (doi:https://doi.org/10.1002/1873-3468.12346) (Full text available)

PDF - Publisher pdf

Creative Commons Licence
This work is licensed under a Creative Commons Attribution 4.0 International License.
Download (512kB) Preview
[img]
Preview
Official URL
http://onlinelibrary.wiley.com/doi/10.1002/1873-34...

Abstract

The dynamic nature of actin polymers is modulated to facilitate a diverse range of cellular processes. These dynamic properties are modulated by different isoforms of Tropomyosin, which are recruited to distinct subpopulations of actin polymers to differentially modulate their functional properties. This makes them 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 non-functional or perturb regulation of actin nucleation and cell cycle timings. Thus conclusions and physiological relevance should be carefully evaluated when using tropomyosin fusions.

Item Type: Article
Uncontrolled keywords: actin, pombe, fission yeast
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 05 Aug 2016 10:13 UTC
Last Modified: 30 Nov 2016 16:41 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/56747 (The current URI for this page, for reference purposes)
  • Depositors only (login required):

Downloads

Downloads per month over past year