Determination of the molecular assembly of actin and actin-binding proteins using photoluminescence.
Colloids Surf B Biointerfaces
; 169: 462-469, 2018 09 01.
Article
em En
| MEDLINE
| ID: mdl-29852435
ABSTRACT
Actin, the most abundant protein in cells, polymerizes into filaments that play key roles in many cellular dynamics. To understand cell dynamics and functions, it is essential to examine the cytoskeleton structure organized by actin and actin-binding proteins. Here, we pave the way for determining the molecular assembly of the actin cytoskeleton using direct photonic in situ analysis, providing the photoluminescence characteristics of actin as a function of filament length and bundling, without labeling. In experiments for monomeric and filamentous actin reconstituted in vitro, structural forms of actin are identified from the peak positions and intensities of photoluminescence. Actin monomers exhibited small intensity emission peaks at 334â¯nm, whereas filamentous and bundled actin showed a shifted peak at 323â¯nm with higher intensity. The peak shift was found to be proportional to the length of the actin filament. With probing structural change of actin in various cells in vivo, our study provides an efficient and precise analytical in situ tool to examine the cytoskeleton structure. It will be beneficial for elucidating the mechanism of various cellular functions such as cell migration, differentiation, cytokinesis and adhesion. Furthermore, our technique can be applied to detect the alterations in the cell cytoskeleton that can occur during many pathological processes.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Actinas
/
Luminescência
/
Proteínas dos Microfilamentos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Colloids Surf B Biointerfaces
Assunto da revista:
QUIMICA
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
Coréia do Sul