Protein Kinase A Regulates Molecular Chaperone Transcription and Protein Aggregation
نویسندگان
چکیده
منابع مشابه
Protein Kinase A Regulates Molecular Chaperone Transcription and Protein Aggregation
Heat shock factor 1 (HSF1) regulates one of the major pathways of protein quality control and is essential for deterrence of protein-folding disorders, particularly in neuronal cells. However, HSF1 activity declines with age, a change that may open the door to progression of neurodegenerative disorders such as Huntington's disease. We have investigated mechanisms of HSF1 regulation that may bec...
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Thr90 phosphorylation of Hsp90α by protein kinase A regulates its chaperone machinery.
Hsp90 (heat-shock protein 90) is one of the most important molecular chaperones in eukaryotes. Hsp90 facilitates the maturation, activation or degradation of its client proteins. It is now well accepted that both ATP binding and co-chaperone association are involved in regulating the Hsp90 chaperone machinery. However, other factors such as post-translational modifications are becoming increasi...
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The chaperone protein network controls both initial protein folding and subsequent maintenance of proteins in the cell. Although the native structure of a protein is principally encoded in its amino acid sequence, the process of folding in vivo very often requires the assistance of molecular chaperones. Chaperones also play a role in a posttranslational quality control system and thus are requi...
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Background Genomic imprinting is a heritable and developmentally essential phenomenon by which gene expression occurs in an allele-specific manner1. While the imprinted alleles are primarily silenced by DNA methylation, it remains largely unknown how methylation is targeted to imprinting control region (ICR), also called differentially methylated region (DMR), and maintained. Here we show that ...
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ژورنال
عنوان ژورنال: PLoS ONE
سال: 2011
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0028950