Constitutive Nuclear Import and Stress-Regulated Nucleocytoplasmic Shuttling of Mammalian Heat-Shock Factor 1
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چکیده
منابع مشابه
Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70.
Heat shock proteins of the hsp/hsc70 family are essential chaperones, implicated in the stress response, aging, and a growing number of human diseases. At the molecular level, hsc70s are required for the proper folding and intracellular targeting of polypeptides as well as the regulation of apoptosis. Cytoplasmic members of the hsp/hsc70 family are believed to shuttle between nuclei and cytopla...
متن کاملStress inhibits the nucleocytoplasmic shuttling of heat shock protein hsc70
Heat shock proteins of the hsp/hsc70 family are essential chaperones, implicated in the stress response, aging, and a growing number of human diseases. At the molecular level, hsc70s are required for the proper folding and intracellular targeting of polypeptides as well as the regulation of apoptosis. Cytoplasmic members of the hsp/hsc70 family are believed to shuttle between nuclei and cytopla...
متن کاملHuman heat shock factor 1 is predominantly a nuclear protein before and after heat stress.
The induction of the heat shock genes in eukaryotes by heat and other forms of stress is mediated by a transcription factor known as heat shock factor 1 (HSF1). HSF1 is present in unstressed metazoan cells as a monomer with low affinity for DNA, and upon exposure to stress it is converted to an 'active' homotrimer that binds the promoters of heat shock genes with high affinity and induces their...
متن کاملEffects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1.
The mammalian heat shock response has been investigated extensively using tissue culture cells with only a limited amount of information available on animals and intact tissues. The neurohormonal stress response mediated by the hypothalamic-pituitary-adrenal axis leads to the activation of heat shock factor (HSF) in rat adrenal tissue. Here we show through the use of antibodies specific to each...
متن کاملThe carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive.
We have characterized a stress-responsive transcriptional activation domain of mouse heat shock factor 1 (HSF1) by using chimeric GAL4-HSF1 fusion proteins. Fusion of the GAL4 DNA-binding domain to residues 124 to 503 of HSF1 results in a chimeric factor that binds DNA yet lacks any transcriptional activity. Transactivation is acquired upon exposure to heat shock or by deletion of a negative re...
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ژورنال
عنوان ژورنال: Traffic
سال: 2005
ISSN: 1398-9219
DOI: 10.1111/j.1600-0854.2005.00266.x