World Library  
Flag as Inappropriate
Email this Article

Hsf2

Article Id: WHEBN0014776902
Reproduction Date:

Title: Hsf2  
Author: World Heritage Encyclopedia
Language: English
Subject: HSF1, Heat shock factor, Transcription factors, NeuroD, EMX homeogene
Collection: Transcription Factors
Publisher: World Heritage Encyclopedia
Publication
Date:
 

Hsf2

Heat shock transcription factor 2
Identifiers
Symbols  ; HSF 2; HSTF 2
External IDs GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Heat shock factor protein 2 is a protein that in humans is encoded by the HSF2 gene.[1][2] HSF2, as well as the related gene HSF1, encodes a protein that binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stresses. Although the names HSF1 and HSF2 were chosen for historical reasons, these peptides should be referred to as heat-shock transcription factors.[2]

Contents

  • Interactions 1
  • See also 2
  • References 3
  • Further reading 4
  • External links 5

Interactions

HSF2 has been shown to interact with Nucleoporin 62[3] and HSF1.[4]

See also

References

  1. ^ Schuetz TJ, Gallo GJ, Sheldon L, Tempst P, Kingston RE (Sep 1991). "Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans". Proc Natl Acad Sci U S A 88 (16): 6911–5.  
  2. ^ a b "Entrez Gene: HSF2 heat shock transcription factor 2". 
  3. ^ Yoshima, T; Yura T; Yanagi H (Nov 1997). "The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62". Biochem. Biophys. Res. Commun. (UNITED STATES) 240 (1): 228–33.  
  4. ^ He, Haiying; Soncin Fabrice; Grammatikakis Nicholas; Li Youlin; Siganou Aliki; Gong Jianlin; Brown Steven A; Kingston Robert E; Calderwood Stuart K (Sep 2003). "Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress". J. Biol. Chem. (United States) 278 (37): 35465–75.  

Further reading

  • Walsh D, Li Z, Wu Y, Nagata K (1997). "Heat shock and the role of the HSPs during neural plate induction in early mammalian CNS and brain development.". Cell. Mol. Life Sci. 53 (2): 198–211.  
  • Sarge KD, Zimarino V, Holm K, et al. (1991). "Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability.". Genes Dev. 5 (10): 1902–11.  
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4.  
  • Sheldon LA, Kingston RE (1993). "Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor 2.". Genes Dev. 7 (8): 1549–58.  
  • Yoshima T, Yura T, Yanagi H (1997). "The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62.". Biochem. Biophys. Res. Commun. 240 (1): 228–33.  
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56.  
  • Yoshima T, Yura T, Yanagi H (1998). "Novel testis-specific protein that interacts with heat shock factor 2.". Gene 214 (1-2): 139–46.  
  • Hong Y, Sarge KD (1999). "Regulation of protein phosphatase 2A activity by heat shock transcription factor 2.". J. Biol. Chem. 274 (19): 12967–70.  
  • Goodson ML, Hong Y, Rogers R, et al. (2001). "Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor.". J. Biol. Chem. 276 (21): 18513–8.  
  • Nykänen P, Alastalo TP, Ahlskog J, et al. (2002). "Genomic organization and promoter analysis of the human heat shock factor 2 gene.". Cell Stress Chaperones 6 (4): 377–85.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903.  
  • He H, Soncin F, Grammatikakis N, et al. (2003). "Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress.". J. Biol. Chem. 278 (37): 35465–75.  
  • Alastalo TP, Hellesuo M, Sandqvist A, et al. (2004). "Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70.". J. Cell. Sci. 116 (Pt 17): 3557–70.  
  • Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11.  
  • Roccisana JL, Kawanabe N, Kajiya H, et al. (2004). "Functional role for heat shock factors in the transcriptional regulation of human RANK ligand gene expression in stromal/osteoblast cells.". J. Biol. Chem. 279 (11): 10500–7.  
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7.  
  • Xing H, Wilkerson DC, Mayhew CN, et al. (2005). "Mechanism of hsp70i gene bookmarking.". Science 307 (5708): 421–3.  
  • Anckar J, Hietakangas V, Denessiouk K, et al. (2006). "Inhibition of DNA binding by differential sumoylation of heat shock factors.". Mol. Cell. Biol. 26 (3): 955–64.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and USA.gov, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for USA.gov and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
 
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
 
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.
 


Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.