Serum response factor

Serum response factor (c-fos serum response element-binding transcription factor)

PDB rendering based on 1hbx.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsSRF ; MCM1
External IDsOMIM: 600589 MGI: 106658 HomoloGene: 31135 GeneCards: SRF Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez672220807
EnsemblENSG00000112658ENSMUSG00000015605
UniProtP11831Q9JM73
RefSeq (mRNA)NM_001292001NM_020493
RefSeq (protein)NP_001278930NP_065239
Location (UCSC)Chr 6:
43.14 – 43.15 Mb		Chr 17:
46.55 – 46.56 Mb
PubMed search

Serum response factor, also known as SRF, is a transcription factor.[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:

References

  1. ↑ Norman C, Runswick M, Pollock R, Treisman R (December 1988). "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. doi:10.1016/0092-8674(88)90244-9. PMID 3203386.
  2. ↑ Shore P, Sharrocks AD (April 1995). "The MADS-box family of transcription factors". Eur. J. Biochem. 229 (1): 1–13. doi:10.1111/j.1432-1033.1995.0001l.x. PMID 7744019.
  3. ↑ Dalton S, Marais R, Wynne J, Treisman R (June 1993). "Isolation and characterization of SRF accessory proteins". Philos. Trans. R. Soc. Lond., B, Biol. Sci. 340 (1293): 325–32. doi:10.1098/rstb.1993.0074. PMID 8103935.
  4. ↑ "SRF serum response factor". Entrez Gene. National Center for Biotechnology Information, National Institutes of Health.
  5. ↑ Sepulveda JL, Vlahopoulos S, Iyer D, Belaguli N, Schwartz RJ (July 2002). "Combinatorial expression of GATA4, Nkx2-5, and serum response factor directs early cardiac gene activity". J. Biol. Chem. 277 (28): 25775–82. doi:10.1074/jbc.M203122200. PMID 11983708.
  6. ↑ Barron MR, Belaguli NS, Zhang SX, Trinh M, Iyer D, Merlo X et al. (March 2005). "Serum response factor, an enriched cardiac mesoderm obligatory factor, is a downstream gene target for Tbx genes". J. Biol. Chem. 280 (12): 11816–28. doi:10.1074/jbc.M412408200. PMID 15591049.
  7. ↑ Li S, Czubryt MP, McAnally J, Bassel-Duby R, Richardson JA, Wiebel FF et al. (January 2005). "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. doi:10.1073/pnas.0409103102. PMC 545866. PMID 15647354.
  8. ↑ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO et al. (March 2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". J. Biol. Chem. 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502.
  9. ↑ Koegel H, von Tobel L, Schäfer M, Alberti S, Kremmer E, Mauch C et al. (April 2009). "Loss of serum response factor in keratinocytes results in hyperproliferative skin disease in mice". J. Clin. Invest. 119 (4): 899–910. doi:10.1172/JCI37771. PMC 2662566. PMID 19307725. Vancouver style error (help)
  10. ↑ Jung DJ, Sung HS, Goo YW, Lee HM, Park OK, Jung SY et al. (July 2002). "Novel transcription coactivator complex containing activating signal cointegrator 1". Mol. Cell. Biol. 22 (14): 5203–11. doi:10.1128/mcb.22.14.5203-5211.2002. PMC 139772. PMID 12077347.
  11. ↑ 11.0 11.1 Zhu C, Johansen FE, Prywes R (September 1997). "Interaction of ATF6 and serum response factor". Mol. Cell. Biol. 17 (9): 4957–66. PMC 232347. PMID 9271374.
  12. ↑ Hanlon M, Sealy L (May 1999). "Ras regulates the association of serum response factor and CCAAT/enhancer-binding protein beta". J. Biol. Chem. 274 (20): 14224–8. doi:10.1074/jbc.274.20.14224. PMID 10318842.
  13. ↑ Sealy L, Malone D, Pawlak M (March 1997). "Regulation of the cfos serum response element by C/EBPbeta". Mol. Cell. Biol. 17 (3): 1744–55. PMC 231899. PMID 9032301.
  14. ↑ 14.0 14.1 Matsuzaki K, Minami T, Tojo M, Honda Y, Saitoh N, Nagahiro S et al. (March 2003). "PML-nuclear bodies are involved in cellular serum response". Genes Cells 8 (3): 275–86. doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724.
  15. ↑ Hassler M, Richmond TJ (June 2001). "The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex". EMBO J. 20 (12): 3018–28. doi:10.1093/emboj/20.12.3018. PMC 150215. PMID 11406578.
  16. ↑ Belaguli NS, Sepulveda JL, Nigam V, Charron F, Nemer M, Schwartz RJ (October 2000). "Cardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulators". Mol. Cell. Biol. 20 (20): 7550–8. doi:10.1128/mcb.20.20.7550-7558.2000. PMC 86307. PMID 11003651.
  17. ↑ Morin S, Paradis P, Aries A, Nemer M (February 2001). "Serum response factor-GATA ternary complex required for nuclear signaling by a G-protein-coupled receptor". Mol. Cell. Biol. 21 (4): 1036–44. doi:10.1128/MCB.21.4.1036-1044.2001. PMC 99558. PMID 11158291.
  18. ↑ Joliot V, Demma M, Prywes R (February 1995). "Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor". Nature 373 (6515): 632–5. doi:10.1038/373632a0. PMID 7854423.
  19. ↑ Zhu H, Joliot V, Prywes R (February 1994). "Role of transcription factor TFIIF in serum response factor-activated transcription". J. Biol. Chem. 269 (5): 3489–97. PMID 8106390.
  20. ↑ Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL et al. (October 1997). "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. doi:10.1101/gad.11.19.2482. PMC 316568. PMID 9334314.
  21. ↑ Kim DW, Cheriyath V, Roy AL, Cochran BH (June 1998). "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Mol. Cell. Biol. 18 (6): 3310–20. PMC 108912. PMID 9584171.
  22. ↑ Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D et al. (March 1996). "Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins". J. Biol. Chem. 271 (9): 5258–64. doi:10.1074/jbc.271.9.5258. PMID 8617811.
  23. ↑ Biesiada E, Hamamori Y, Kedes L, Sartorelli V (April 1999). "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. PMC 84050. PMID 10082523.
  24. ↑ Yamada K, Osawa H, Granner DK (October 1999). "Identification of proteins that interact with NF-YA". FEBS Lett. 460 (1): 41–5. doi:10.1016/s0014-5793(99)01311-3. PMID 10571058.
  25. ↑ Lee SK, Kim JH, Lee YC, Cheong J, Lee JW (April 2000). "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. doi:10.1074/jbc.275.17.12470. PMID 10777532.
  26. ↑ Kim HJ, Kim JH, Lee JW (October 1998). "Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations". J. Biol. Chem. 273 (44): 28564–7. doi:10.1074/jbc.273.44.28564. PMID 9786846.
  27. ↑ Gupta M, Kogut P, Davis FJ, Belaguli NS, Schwartz RJ, Gupta MP (March 2001). "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. doi:10.1074/jbc.M008625200. PMID 11136726.

External links

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