Literature DB >> 10413683

Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress.

P A Mercier1, N A Winegarden, J T Westwood.   

Abstract

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 transcription. The conversion of HSF1 to its active form is hypothesized to be a multistep process involving physical changes in the HSF1 molecule and the possible translocation of HSF1 from the cytoplasm to the nucleus. While all studies to date have found active HSF1 to be a nuclear protein, there have been conflicting reports on whether the inactive form of HSF is predominantly a cytoplasmic or nuclear protein. In this study, we have made antibodies against human HSF1 and have reexamined its localization in unstressed and heat-shocked human HeLa and A549 cells, and in green monkey Vero cells. Biochemical fractionation of heat-shocked HeLa cells followed by western blot analysis showed that HSF1 was mostly found in the nuclear fraction. In extracts made from unshocked cells, HSF1 was predominantly found in the cytoplasmic fraction using one fractionation procedure, but was distributed approximately equally between the cytoplasmic and nuclear fractions when a different procedure was used. Immunofluorescence microscopy revealed that HSF1 was predominantly a nuclear protein in both heat shocked and unstressed cells. Quantification of HSF1 staining showed that approximately 80% of HSF1 was present in the nucleus both before and after heat stress. These results suggest that HSF1 is predominantly a nuclear protein prior to being exposed to stress, but has low affinity for the nucleus and is easily extracted using most biochemical fractionation procedures. These results also imply that HSF1 translocation is probably not part of the multistep process in HSF1 activation for many cell types.

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Year:  1999        PMID: 10413683     DOI: 10.1242/jcs.112.16.2765

Source DB:  PubMed          Journal:  J Cell Sci        ISSN: 0021-9533            Impact factor:   5.285


  25 in total

1.  A pyrrole-based natural small molecule mitigates HSP90 expression in MDA-MB-231 cells and inhibits tumor angiogenesis in mice by inactivating HSF-1.

Authors:  K C Rashmi; H S Atreya; M Harsha Raj; Bharathi P Salimath; H S Aparna
Journal:  Cell Stress Chaperones       Date:  2017-07-17       Impact factor: 3.667

2.  SAGA and Rpd3 chromatin modification complexes dynamically regulate heat shock gene structure and expression.

Authors:  Selena B Kremer; David S Gross
Journal:  J Biol Chem       Date:  2009-09-15       Impact factor: 5.157

3.  Dual neuroprotective pathways of a pro-electrophilic compound via HSF-1-activated heat-shock proteins and Nrf2-activated phase 2 antioxidant response enzymes.

Authors:  Takumi Satoh; Tayebeh Rezaie; Masaaki Seki; Carmen R Sunico; Takahito Tabuchi; Tomomi Kitagawa; Mika Yanagitai; Mutsumi Senzaki; Chihiro Kosegawa; Hideharu Taira; Scott R McKercher; Jennifer K Hoffman; Gregory P Roth; Stuart A Lipton
Journal:  J Neurochem       Date:  2011-09-21       Impact factor: 5.372

4.  Modulation of Drosophila heat shock transcription factor activity by the molecular chaperone DROJ1.

Authors:  G Marchler; C Wu
Journal:  EMBO J       Date:  2001-02-01       Impact factor: 11.598

5.  HSF-1 regulators DDL-1/2 link insulin-like signaling to heat-shock responses and modulation of longevity.

Authors:  Wei-Chung Chiang; Tsui-Ting Ching; Hee Chul Lee; Carol Mousigian; Ao-Lin Hsu
Journal:  Cell       Date:  2012-01-20       Impact factor: 41.582

6.  Structure of human heat-shock transcription factor 1 in complex with DNA.

Authors:  Tobias Neudegger; Jacob Verghese; Manajit Hayer-Hartl; F Ulrich Hartl; Andreas Bracher
Journal:  Nat Struct Mol Biol       Date:  2016-01-04       Impact factor: 15.369

Review 7.  Regulation of heat shock transcription factors and their roles in physiology and disease.

Authors:  Rocio Gomez-Pastor; Eileen T Burchfiel; Dennis J Thiele
Journal:  Nat Rev Mol Cell Biol       Date:  2017-08-30       Impact factor: 94.444

8.  Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1.

Authors:  XiaoZhe Wang; Nicholas Grammatikakis; Aliki Siganou; Stuart K Calderwood
Journal:  Mol Cell Biol       Date:  2003-09       Impact factor: 4.272

9.  Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions.

Authors:  Wesley J Hung; Rachel S Roberson; Jaime Taft; Daniel Y Wu
Journal:  Mol Cell Biol       Date:  2003-05       Impact factor: 4.272

10.  Caenorhabditis elegans HSF-1 is an essential nuclear protein that forms stress granule-like structures following heat shock.

Authors:  Elizabeth A Morton; Todd Lamitina
Journal:  Aging Cell       Date:  2012-11-23       Impact factor: 9.304

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