| Autor: |
Arrigo AP; Cancer and Development Laboratory, Lyon Cancer Research Center, Centre Léon Bérard, UMR INSERM 1052-CNRS 5286, Claude Bernard University, 28 rue Laennec, Lyon, 69008, France. arrigo@univ-lyon1.fr. |
| Jazyk: |
angličtina |
| Zdroj: |
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2018; Vol. 1709, pp. 163-178. |
| DOI: |
10.1007/978-1-4939-7477-1_12 |
| Abstrakt: |
Human HspB1 (also denoted as Hsp27) belongs to the family of small (or stress) proteins (sHsps). The family, which contains ten members including αA,B-crystallin polypeptides, is characterized by a conserved C-terminal α-crystallin domain and molecular weights ranging from 20 to 40 kDa. Here, procedures are described for analyzing the dynamic oligomerization and phosphorylation patterns of HspB1 in cells exposed to different environments. Changes in the structural organization of HspB1 can reprogram its interaction with specific partner/client polypeptides. Methods are presented to analyze these interactions using tissue culture cells genetically modified to express different levels of this protein. In addition, the laboratory approaches presented here could be used to test the nine other human sHsp members as well as sHsps from other species. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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