HSF1

HSF1
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	2LDU, 5D5U, 5D5V
Identificadores
Nomes alternativos	HSF1, Fator de choque térmico 1
IDs externos	OMIM: 140580 HomoloGene: 74556 GeneCards: HSF1
Ontologia genética
Função molecular	• GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity; • chromatin binding; • GO:0001078, GO:0001214, GO:0001206 DNA-binding transcription repressor activity, RNA polymerase II-specific; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; • sequence-specific single stranded DNA binding; • DNA binding; • protein kinase binding; • heat shock protein binding; • chromatin DNA binding; • identical protein binding; • sequence-specific DNA binding; • protein self-association; • protein heterodimerization activity; • Hsp90 protein binding; • translation elongation factor binding; • promoter-specific chromatin binding; • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding; • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific; • STAT family protein binding;
Componente celular	• citoplasma; • pronúcleo; • GO:0035327 eucromatina; • GO:0035328 heterocromatina; • núcleo celular; • centrossoma; • citosol; • PML body; • nuclear stress granule; • mitotic spindle pole; • partículas de ribonucleoproteínas heterogéneas; • centrómero; • cinetócoro; • spindle pole; • cariolinfa; • cromossoma; • centro organizador dos microtúbulos; • citoesqueleto; • perinuclear region of cytoplasm; • GO:0009327 complexo macromolecular;
Processo biológico	• defense response; • GO:0009373 regulation of transcription, DNA-templated; • embryonic placenta development; • mRNA transcription; • in utero embryonic development; • GO:1901227 negative regulation of transcription by RNA polymerase II; • response to heat; • female meiotic nuclear division; • transcription, DNA-templated; • embryonic process involved in female pregnancy; • protein phosphorylation; • response to lipopolysaccharide; • espermatogênese; • positive regulation of multicellular organism growth; • negative regulation of tumor necrosis factor production; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • negative regulation of cell population proliferation; • response to organonitrogen compound; • cellular response to lipopolysaccharide; • negative regulation of gene expression; • cellular response to amino acid stimulus; • cellular response to hydrogen peroxide; • positive regulation of microtubule binding; • response to peptide; • cellular response to nitroglycerin; • negative regulation of cardiac muscle cell apoptotic process; • response to estradiol; • GO:1904579 cellular response to organic cyclic compound; • GO:1901313 positive regulation of gene expression; • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; • cellular response to potassium ion; • response to amino acid; • negative regulation of inclusion body assembly; • positive regulation of apoptotic DNA fragmentation; • cellular response to L-glutamine; • response to psychosocial stress; • GO:1904578 response to organic cyclic compound; • negative regulation of neuron death; • response to nutrient; • cellular response to angiotensin; • response to testosterone; • response to hypobaric hypoxia; • response to activity; • cellular response to radiation; • cellular response to estradiol stimulus; • positive regulation of inclusion body assembly; • MAPK cascade; • positive regulation of cell population proliferation; • cellular response to heat; • Unfolded protein response; • regulation of protein heterodimerization activity; • positive regulation of mitotic cell cycle; • protein homooligomerization; • positive regulation of transcription from RNA polymerase II promoter in response to heat stress; • protein homotrimerization; • cellular response to cadmium ion; • cellular response to copper ion; • cellular response to gamma radiation; • cellular response to diamide; • regulation of cellular response to heat; • positive regulation of mRNA polyadenylation; • cellular response to sodium arsenite; • negative regulation of double-strand break repair via nonhomologous end joining; • GO:0100026 reparo de ADN; • mRNA processing; • cellular response to DNA damage stimulus; • mRNA transport; • positive regulation of tyrosine phosphorylation of STAT protein; • positive regulation of cold-induced thermogenesis;
	Sources:Amigo / QuickGO
Ortólogos
	3297
	n/a
	ENSG00000185122; ENSG00000284774
	n/a
	Q00613
	n/a
	NM_005526
	n/a
	NP_005517
	n/a
	Wikidata
Ver/Editar Humano

Fator de choque térmico 1 é uma proteína que em humanos é codificada pelo gene HSF1.

Função

O HSF1, assim como o gene relacionado HSF2, codifica uma proteína que se liga especificamente ao elemento de choque térmico e é altamente conservado em eucariotos e é o mediador primário das respostas transcricionais ao estresse proteotóxico, com papéis importantes na regulação não relacionada ao estresse, como o desenvolvimento e o metabolismo.

Referências

↑ «Human PubMed Reference:»
↑ Rabindran SK, Giorgi G, Clos J, Wu C (agosto de 1991). «Molecular cloning and expression of a human heat shock factor, HSF1». Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 6906–10. PMC 52202. PMID 1871105. doi:10.1073/pnas.88.16.6906
↑ Vihervaara A, Sistonen L (janeiro de 2014). «HSF1 at a glance». Journal of Cell Science (em inglês). 127 (Pt 2): 261–6. PMID 24421309. doi:10.1242/jcs.132605
↑ Anckar J, Sistonen L (15 de junho de 2011). «Regulation of HSF1 function in the heat stress response: implications in aging and disease». Annual Review of Biochemistry (em inglês). 80 (1): 1089–115. PMID 21417720. doi:10.1146/annurev-biochem-060809-095203

Leitura adicional

Voellmy R (1996). Sensing stress and responding to stress. Exs. 77. [S.l.: s.n.] pp. 121–37. ISBN 978-3-0348-9901-7. PMID 8856972. doi:10.1007/978-3-0348-9088-5_9
Abravaya K, Myers MP, Murphy SP, Morimoto RI (julho de 1992). «The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression». Genes & Development. 6 (7): 1153–64. PMID 1628823. doi:10.1101/gad.6.7.1153
Schuetz TJ, Gallo GJ, Sheldon L, Tempst P, Kingston RE (agosto de 1991). «Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans». Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 6911–5. PMC 52203. PMID 1871106. doi:10.1073/pnas.88.16.6911
Nunes SL, Calderwood SK (agosto de 1995). «Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells». Biochemical and Biophysical Research Communications. 213 (1): 1–6. PMID 7639722. doi:10.1006/bbrc.1995.2090
Maruyama K, Sugano S (janeiro de 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
Chu B, Soncin F, Price BD, Stevenson MA, Calderwood SK (novembro de 1996). «Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1». The Journal of Biological Chemistry. 271 (48): 30847–57. PMID 8940068. doi:10.1074/jbc.271.48.30847
Fukunaga R, Hunter T (abril de 1997). «MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates». The EMBO Journal. 16 (8): 1921–33. PMC 1169795. PMID 9155018. doi:10.1093/emboj/16.8.1921
Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF (dezembro de 1996). «A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor». Cell Stress & Chaperones. 1 (4): 237–50. PMC 376461. PMID 9222609. doi:10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2
Huang J, Nueda A, Yoo S, Dynan WS (outubro de 1997). «Heat shock transcription factor 1 binds selectively in vitro to Ku protein and the catalytic subunit of the DNA-dependent protein kinase». The Journal of Biological Chemistry. 272 (41): 26009–16. PMID 9325337. doi:10.1074/jbc.272.41.26009
Cotto J, Fox S, Morimoto R (dezembro de 1997). «HSF1 granules: a novel stress-induced nuclear compartment of human cells». Journal of Cell Science. 110 ( Pt 23) (23): 2925–34. PMID 9359875
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (outubro de 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
Shi Y, Mosser DD, Morimoto RI (março de 1998). «Molecular chaperones as HSF1-specific transcriptional repressors». Genes & Development. 12 (5): 654–66. PMC 316571. PMID 9499401. doi:10.1101/gad.12.5.654
Satyal SH, Chen D, Fox SG, Kramer JM, Morimoto RI (julho de 1998). «Negative regulation of the heat shock transcriptional response by HSBP1». Genes & Development. 12 (13): 1962–74. PMC 316975. PMID 9649501. doi:10.1101/gad.12.13.1962
Zhou X, Tron VA, Li G, Trotter MJ (agosto de 1998). «Heat shock transcription factor-1 regulates heat shock protein-72 expression in human keratinocytes exposed to ultraviolet B light». The Journal of Investigative Dermatology. 111 (2): 194–8. PMID 9699716. doi:10.1046/j.1523-1747.1998.00266.x
Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (agosto de 1998). «Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1». Cell. 94 (4): 471–80. PMID 9727490. doi:10.1016/S0092-8674(00)81588-3
Stephanou A, Isenberg DA, Nakajima K, Latchman DS (janeiro de 1999). «Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90beta gene promoters». The Journal of Biological Chemistry. 274 (3): 1723–8. PMID 9880553. doi:10.1074/jbc.274.3.1723
Dai R, Frejtag W, He B, Zhang Y, Mivechi NF (junho de 2000). «c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity». The Journal of Biological Chemistry. 275 (24): 18210–8. PMID 10747973. doi:10.1074/jbc.M000958200
Choi Y, Asada S, Uesugi M (maio de 2000). «Divergent hTAFII31-binding motifs hidden in activation domains». The Journal of Biological Chemistry. 275 (21): 15912–6. PMID 10821850. doi:10.1074/jbc.275.21.15912

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[1] «Human PubMed Reference:»

[pmid18711052-2] Rabindran SK, Giorgi G, Clos J, Wu C (agosto de 1991). «Molecular cloning and expression of a human heat shock factor, HSF1». Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 6906–10. PMC 52202. PMID 1871105. doi:10.1073/pnas.88.16.6906

[3] Vihervaara A, Sistonen L (janeiro de 2014). «HSF1 at a glance». Journal of Cell Science (em inglês). 127 (Pt 2): 261–6. PMID 24421309. doi:10.1242/jcs.132605

[:02-4] Anckar J, Sistonen L (15 de junho de 2011). «Regulation of HSF1 function in the heat stress response: implications in aging and disease». Annual Review of Biochemistry (em inglês). 80 (1): 1089–115. PMID 21417720. doi:10.1146/annurev-biochem-060809-095203