STAT1

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Преобразователь сигнала и активатор транскрипции 1, 91kDa
Stat1 stucture.png
STAT1 bound to DNA
Доступные структуры
PDB Поиск ортологов: PDBe, RCSB
Идентификаторы
Символ STAT1 ; CANDF7; ISGF-3; STAT91
Внешние ID OMIM: 600555 MGI103063 HomoloGene21428 ChEMBL: 6101 GeneCards: STAT1 Gene
Профиль экспрессии РНК
PBB GE STAT1 200887 s at tn.png
Больше информации
Ортологи
Вид Человек Мышь
Entrez 6772 20846
Ensembl ENSG00000115415 ENSMUSG00000026104
UniProt P42224 P42225
RefSeq (мРНК) NM_007315 NM_001205313
RefSeq (белок) NP_009330 NP_001192242
Локус (UCSC) Chr 2:
191.83 – 191.89 Mb
Chr 1:
52.12 – 52.16 Mb
Поиск в PubMed [1] [2]

STAT1 является членом семейства транскрипционных факторов преобразователей сигналов и активаторов транскрипции[en] . STAT1 участвует в положительной регуляции генов по сигналам интерферона либо типа I, типа II, или типа III. В ответ на IFN-γ стимуляцию, STAT1 образует гомодимеры или гетеродимеры с STAT3, которые связываются с GAS (Interferon G amma- A ctivated S equence) промоторным элементом; В ответ на любую IFN-α или IFN-β стимуляцию, STAT1 образует гетеродимер с STAT2, который может связываться с ISRE ( I nterferon- S timulated R esponse E lement) промоторным элементом.[1] В любом случае, связывание элемента с промотором приводит к увеличению экспрессии ISG ( I nterferon- S timulated G enes).

Выражение STAT1 можно индуцировать в соединении с Диаллилдисульфидом в чеснок.[2]

Взаимодействия[править | править вики-текст]

STAT1 было показано, взаимодействуют с:

Примечания[править | править вики-текст]

  1. (2002) «Viruses and interferon: a fight for supremacy». Nature Reviews Immunology 2 (9): 675–87. DOI:10.1038/nri888. PMID 12209136.
  2. (2007) «Diallyl disulfide induced signal transducer and activator of transcription 1 expression in human colon cancer colo 205 cells using differential display RT-PCR». Cancer Genomics Proteomics. 4 (2): 93–7. PMID 17804871.
  3. (May 2000) «Collaboration of signal transducer and activator of transcription 1 (STAT1) and BRCA1 in differential regulation of IFN-gamma target genes». Proc. Natl. Acad. Sci. U.S.A. 97 (10): 5208-13. DOI:10.1073/pnas.080469697. PMID 10792030.
  4. (October 1999) «Interacting regions in Stat3 and c-Jun that participate in cooperative transcriptional activation». Mol. Cell. Biol. 19 (10): 7138-46. PMID 10490649.
  5. (October 1997) «Stat1 associates with c-kit and is activated in response to stem cell factor». Biochem. J. 327 ( Pt 1): 73-80. PMID 9355737.
  6. (Dec 1996) «Two contact regions between Stat1 and CBP/p300 in interferon gamma signaling». Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15092-6. PMID 8986769.
  7. (April 2002) «Stat1-vitamin D receptor interactions antagonize 1,25-dihydroxyvitamin D transcriptional activity and enhance stat1-mediated transcription». Mol. Cell. Biol. 22 (8): 2777-87. PMID 11909970.
  8. 1 2 (June 1999) «ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases». J. Biol. Chem. 274 (24): 17209-18. PMID 10358079.
  9. 1 2 (August 2002) «Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation». J. Biol. Chem. 277 (34): 30716-23. DOI:10.1074/jbc.M202823200. PMID 12070153.
  10. (July 2000) «The Fanconi anemia protein FANCC binds to and facilitates the activation of STAT1 by gamma interferon and hematopoietic growth factors». Mol. Cell. Biol. 20 (13): 4724-35. PMID 10848598.
  11. (October 2003) «Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport». Exp. Cell Res. 289 (2): 211-21. PMID 14499622.
  12. (September 2001) «The Fanconi anemia complementation group C gene product: structural evidence of multifunctionality». Blood 98 (5): 1392-401. PMID 11520787.
  13. 1 2 (June 2001) «The WD motif-containing protein receptor for activated protein kinase C (RACK1) is required for recruitment and activation of signal transducer and activator of transcription 1 through the type I interferon receptor». J. Biol. Chem. 276 (25): 22948-53. DOI:10.1074/jbc.M100087200. PMID 11301323.
  14. (September 2003) «The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex». J. Immunol. 171 (6): 2989-94. PMID 12960323.
  15. (April 1997) «Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling». Mol. Cell. Biol. 17 (4): 2048-56. PMID 9121453.
  16. (July 2000) «Adenovirus E1A down-regulates LMP2 transcription by interfering with the binding of stat1 to IRF1». J. Biol. Chem. 275 (27): 20406-11. DOI:10.1074/jbc.M001861200. PMID 10764778.
  17. (Dec 1996) «Interactions between STAT and non-STAT proteins in the interferon-stimulated gene factor 3 transcription complex». Mol. Cell. Biol. 16 (12): 6957-64. PMID 8943351.
  18. (May 2003) «Cutting edge: role of IL-27/WSX-1 signaling for induction of T-bet through activation of STAT1 during initial Th1 commitment». J. Immunol. 170 (10): 4886-90. PMID 12734330.
  19. (Dec 1998) «Ser727-dependent recruitment of MCM5 by Stat1alpha in IFN-gamma-induced transcriptional activation». EMBO J. 17 (23): 6963-71. DOI:10.1093/emboj/17.23.6963. PMID 9843502.
  20. (March 2001) «Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-gamma». Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3034-9. DOI:10.1073/pnas.061487598. PMID 11248027.
  21. 1 2 (September 2003) «Stimulation of signal transducer and activator of transcription-1 (STAT1)-dependent gene transcription by lipopolysaccharide and interferon-gamma is regulated by mammalian target of rapamycin». J. Biol. Chem. 278 (36): 33637-44. DOI:10.1074/jbc.M301053200. PMID 12807916.
  22. (May 2000) «Distinct roles of the NH2- and COOH-terminal domains of the protein inhibitor of activated signal transducer and activator of transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1-Stat1 interaction». Proc. Natl. Acad. Sci. U.S.A. 97 (10): 5267-72. PMID 10805787.
  23. (June 2001) «Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion». J. Biol. Chem. 276 (22): 19512-23. DOI:10.1074/jbc.M009063200. PMID 11278462.
  24. (March 1997) «Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways». EMBO J. 16 (6): 1291-304. DOI:10.1093/emboj/16.6.1291. PMID 9135145.
  25. (April 2001) «Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR». J. Biol. Chem. 276 (17): 13727-37. DOI:10.1074/jbc.M011240200. PMID 11278865.
  26. (March 1996) «Formation of STAT1-STAT2 heterodimers and their role in the activation of IRF-1 gene transcription by interferon-alpha». J. Biol. Chem. 271 (10): 5790-4. PMID 8621447.
  27. (August 1999) «Urokinase induces activation and formation of Stat4 and Stat1-Stat2 complexes in human vascular smooth muscle cells». J. Biol. Chem. 274 (34): 24059-65. PMID 10446176.
  28. (August 2002) «Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin alpha 5». J. Biol. Chem. 277 (33): 30072-8. DOI:10.1074/jbc.M202943200. PMID 12048190.
  29. (October 2001) «Involvement of tyrosine phosphatase PTP1D in the inhibition of interleukin-6-induced Stat3 signaling by alpha-thrombin». Biochem. Biophys. Res. Commun. 288 (1): 252-7. DOI:10.1006/bbrc.2001.5759. PMID 11594781.
  30. (August 2001) «Constitutive activation of STAT transcription factors in acute myelogenous leukemia». Eur. J. Haematol. 67 (2): 63-71. PMID 11722592.
  31. (October 1997) «c-Src activates both STAT1 and STAT3 in PDGF-stimulated NIH3T3 cells». Biochem. Biophys. Res. Commun. 239 (2): 493-7. DOI:10.1006/bbrc.1997.7493. PMID 9344858.
  32. (July 2000) «Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation». Mol. Cell. Biol. 20 (13): 4505-12. PMID 10848577.