Biology:Serum response factor

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Short description: Mammalian protein found in Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Serum response factor, also known as SRF, is a transcription factor protein.[1]

Function

Serum response factor is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors.[2] This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs).[3][4]

SRF is important during the development of the embryo, as it has been linked to the formation of mesoderm.[5][6] In the fully developed mammal, SRF is crucial for the growth of skeletal muscle.[7] Interaction of SRF with other proteins, such as steroid hormone receptors, may contribute to regulation of muscle growth by steroids.[8] Interaction of SRF with other proteins such as myocardin or Elk-1 may enhance or suppress expression of genes important for growth of vascular smooth muscle.

Clinical significance

Lack of skin SRF is associated with psoriasis and other skin diseases.[9]

Interactions

Serum response factor has been shown to interact with:


See also

References

  1. ↑ "Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element". Cell 55 (6): 989–1003. December 1988. doi:10.1016/0092-8674(88)90244-9. PMID 3203386. 
  2. ↑ "The MADS-box family of transcription factors". Eur. J. Biochem. 229 (1): 1–13. April 1995. doi:10.1111/j.1432-1033.1995.0001l.x. PMID 7744019. 
  3. ↑ "Isolation and characterization of SRF accessory proteins". Philos. Trans. R. Soc. Lond. B Biol. Sci. 340 (1293): 325–32. June 1993. doi:10.1098/rstb.1993.0074. PMID 8103935. Bibcode: 1993RSPTB.340..325D. 
  4. ↑ "SRF serum response factor". Entrez Gene. National Center for Biotechnology Information, National Institutes of Health. https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6722. 
  5. ↑ "Combinatorial expression of GATA4, Nkx2-5, and serum response factor directs early cardiac gene activity". J. Biol. Chem. 277 (28): 25775–82. July 2002. doi:10.1074/jbc.M203122200. PMID 11983708. 
  6. ↑ "Serum response factor, an enriched cardiac mesoderm obligatory factor, is a downstream gene target for Tbx genes". J. Biol. Chem. 280 (12): 11816–28. March 2005. doi:10.1074/jbc.M412408200. PMID 15591049. 
  7. ↑ "Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice". Proc. Natl. Acad. Sci. U.S.A. 102 (4): 1082–7. January 2005. doi:10.1073/pnas.0409103102. PMID 15647354. Bibcode: 2005PNAS..102.1082L. 
  8. ↑ "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". J. Biol. Chem. 280 (9): 7786–92. March 2005. doi:10.1074/jbc.M413992200. PMID 15623502. 
  9. ↑ "Loss of serum response factor in keratinocytes results in hyperproliferative skin disease in mice". J. Clin. Invest. 119 (4): 899–910. April 2009. doi:10.1172/JCI37771. PMID 19307725. 
  10. ↑ "Novel transcription coactivator complex containing activating signal cointegrator 1". Mol. Cell. Biol. 22 (14): 5203–11. July 2002. doi:10.1128/mcb.22.14.5203-5211.2002. PMID 12077347. 
  11. ↑ 11.0 11.1 "Interaction of ATF6 and serum response factor". Mol. Cell. Biol. 17 (9): 4957–66. September 1997. doi:10.1128/MCB.17.9.4957. PMID 9271374. 
  12. ↑ "Ras regulates the association of serum response factor and CCAAT/enhancer-binding protein beta". J. Biol. Chem. 274 (20): 14224–8. May 1999. doi:10.1074/jbc.274.20.14224. PMID 10318842. 
  13. ↑ "Regulation of the cfos serum response element by C/EBPbeta". Mol. Cell. Biol. 17 (3): 1744–55. March 1997. doi:10.1128/mcb.17.3.1744. PMID 9032301. 
  14. ↑ 14.0 14.1 "PML-nuclear bodies are involved in cellular serum response". Genes Cells 8 (3): 275–86. March 2003. doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724. 
  15. ↑ "The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex". EMBO J. 20 (12): 3018–28. June 2001. doi:10.1093/emboj/20.12.3018. PMID 11406578. 
  16. ↑ "Cardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulators". Mol. Cell. Biol. 20 (20): 7550–8. October 2000. doi:10.1128/mcb.20.20.7550-7558.2000. PMID 11003651. 
  17. ↑ "Serum response factor-GATA ternary complex required for nuclear signaling by a G-protein-coupled receptor". Mol. Cell. Biol. 21 (4): 1036–44. February 2001. doi:10.1128/MCB.21.4.1036-1044.2001. PMID 11158291. 
  18. ↑ "Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor". Nature 373 (6515): 632–5. February 1995. doi:10.1038/373632a0. PMID 7854423. Bibcode: 1995Natur.373..632J. 
  19. ↑ "Role of transcription factor TFIIF in serum response factor-activated transcription". J. Biol. Chem. 269 (5): 3489–97. February 1994. doi:10.1016/S0021-9258(17)41889-8. PMID 8106390. 
  20. ↑ "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I". Genes Dev. 11 (19): 2482–93. October 1997. doi:10.1101/gad.11.19.2482. PMID 9334314. 
  21. ↑ "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Mol. Cell. Biol. 18 (6): 3310–20. June 1998. doi:10.1128/mcb.18.6.3310. PMID 9584171. 
  22. ↑ "Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins". J. Biol. Chem. 271 (9): 5258–64. March 1996. doi:10.1074/jbc.271.9.5258. PMID 8617811. 
  23. ↑ "Myogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoter". Mol. Cell. Biol. 19 (4): 2577–84. April 1999. doi:10.1128/MCB.19.4.2577. PMID 10082523. 
  24. ↑ "Identification of proteins that interact with NF-YA". FEBS Lett. 460 (1): 41–5. October 1999. doi:10.1016/s0014-5793(99)01311-3. PMID 10571058. 
  25. ↑ "Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor". J. Biol. Chem. 275 (17): 12470–4. April 2000. doi:10.1074/jbc.275.17.12470. PMID 10777532. 
  26. ↑ "Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations". J. Biol. Chem. 273 (44): 28564–7. October 1998. doi:10.1074/jbc.273.44.28564. PMID 9786846. 
  27. ↑ "Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1". J. Biol. Chem. 276 (13): 10413–22. March 2001. doi:10.1074/jbc.M008625200. PMID 11136726. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine ([1]), which is in the public domain.



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