EurekaMag.com logo
+ Site Statistics
References:
53,214,146
Abstracts:
29,074,682
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and Its Interaction with Specific Client Polypeptides


Methods in Molecular Biology 1709: 163-178
Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and Its Interaction with Specific Client Polypeptides
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.

(PDF same-day service: $19.90)

Accession: 046800728

PMID: 29177658

DOI: 10.1007/978-1-4939-7477-1_12



Related references

The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Molecular and Cellular Endocrinology 270(1-2): 33-42, 2007

The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization. European Journal of Biochemistry 221(1): 327-334, 1994

Analysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1). Plos One 8(8): E70545-E70545, 2014

Effect of proteasome inhibition by MG-132 on HSP27 oligomerization, phosphorylation, and aggresome formation in the OLN-93 oligodendroglia cell line. Journal of Neurochemistry 114(4): 960-971, 2010

HSP27 in Sertoli cells Germ cell-stimulated HSP27 phosphorylation, mRNA levels during spermato-genesis, and HSP27 co-localization with microfilaments. Journal of Cellular Biochemistry Supplement 0(19B): 206, 1995

Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor a by phosphorylation. The Journal of Biological Chemistry 274(27): 947-56, 1999

Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. Journal of Biological Chemistry 274(27): 18947-18956, 1999

Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1. Journal of Biological Chemistry 292(24): 9944-9957, 2017

Structure-functions of HspB1 (Hsp27). Methods in Molecular Biology 787: 105-119, 2012

3,4-DGE is cytotoxic and decreases HSP27/HSPB1 in podocytes. Archives of Toxicology 88(3): 597-608, 2015