HSF2
Proteína do fator de choque térmico 2 é uma proteína que em humanos é codificada pelo gene HSF2.[2][3]
Função[editar | editar código-fonte]
O HSF2, assim como o gene relacionado HSF1, codifica uma proteína que se liga especificamente ao elemento de choque térmico e tem homologia com os HSFs de outras espécies. Fatores de transcrição de choque térmico ativam genes de resposta ao choque térmico sob condições de calor ou outras tensões. Embora os nomes HSF1 e HSF2 tenham sido escolhidos por razões históricas, esses peptídeos devem ser referidos como fatores de transcrição de choque térmico.[3]
Interações[editar | editar código-fonte]
Demonstrou-se que o HSF2 interage com a nucleoporina 62[4] e o HSF1.[5]
Referências
- ↑ «Human PubMed Reference:»
- ↑ Schuetz TJ, Gallo GJ, Sheldon L, Tempst P, Kingston RE (setembro de 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. PMC 52203. PMID 1871106. doi:10.1073/pnas.88.16.6911
- ↑ a b «Entrez Gene: HSF2 heat shock transcription factor 2»
- ↑ Yoshima T, Yura T, Yanagi H (novembro de 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. PMID 9367915. doi:10.1006/bbrc.1997.7662
- ↑ He H, Soncin F, Grammatikakis N, Li Y, Siganou A, Gong J, Brown SA, Kingston RE, Calderwood SK (setembro de 2003). «Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress». J. Biol. Chem. 278 (37): 35465–75. PMID 12813038. doi:10.1074/jbc.M304663200
Leitura adicional[editar | editar código-fonte]
- 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. PMID 9118008. doi:10.1007/PL00000592
- Sarge KD, Zimarino V, Holm K, Wu C, Morimoto RI (1991). «Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability.». Genes Dev. 5 (10): 1902–11. PMID 1717345. doi:10.1101/gad.5.10.1902
- 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. PMID 8125298. doi:10.1016/0378-1119(94)90802-8
- 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. PMID 8339932. doi:10.1101/gad.7.8.1549
- 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. PMID 9367915. doi:10.1006/bbrc.1997.7662
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). «Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.». Gene. 200 (1–2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3
- Yoshima T, Yura T, Yanagi H (1998). «Novel testis-specific protein that interacts with heat shock factor 2.». Gene. 214 (1–2): 139–46. PMID 9651507. doi:10.1016/S0378-1119(98)00208-X
- Hong Y, Sarge KD (1999). «Regulation of protein phosphatase 2A activity by heat shock transcription factor 2.». J. Biol. Chem. 274 (19): 12967–70. PMID 10224043. doi:10.1074/jbc.274.19.12967
- Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD (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. PMID 11278381. doi:10.1074/jbc.M008066200
- Nykänen P, Alastalo TP, Ahlskog J, Horelli-Kuitunen N, Pirkkala L, Sistonen L (2002). «Genomic organization and promoter analysis of the human heat shock factor 2 gene.». Cell Stress Chaperones. 6 (4): 377–85. PMC 434421. PMID 11795475. doi:10.1379/1466-1268(2001)006<0377:GOAPAO>2.0.CO;2
- He H, Soncin F, Grammatikakis N, Li Y, Siganou A, Gong J, Brown SA, Kingston RE, Calderwood SK (2003). «Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress.». J. Biol. Chem. 278 (37): 35465–75. PMID 12813038. doi:10.1074/jbc.M304663200
- Alastalo TP, Hellesuo M, Sandqvist A, Hietakangas V, Kallio M, Sistonen L (2004). «Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70.». J. Cell Sci. 116 (Pt 17): 3557–70. PMID 12865437. doi:10.1242/jcs.00671
- Roccisana JL, Kawanabe N, Kajiya H, Koide M, Roodman GD, Reddy SV (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. PMID 14699143. doi:10.1074/jbc.M303727200
- Xing H, Wilkerson DC, Mayhew CN, Lubert EJ, Skaggs HS, Goodson ML, Hong Y, Park-Sarge OK, Sarge KD (2005). «Mechanism of hsp70i gene bookmarking.». Science. 307 (5708): 421–3. PMID 15662014. doi:10.1126/science.1106478
- Anckar J, Hietakangas V, Denessiouk K, Thiele DJ, Johnson MS, Sistonen L (2006). «Inhibition of DNA binding by differential sumoylation of heat shock factors.». Mol. Cell. Biol. 26 (3): 955–64. PMC 1347039. PMID 16428449. doi:10.1128/MCB.26.3.955-964.2006