From Wikipedia, the free encyclopedia
SRF
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases SRF, MCM1, serum response factor
External IDs OMIM: 600589 MGI: 106658 HomoloGene: 31135 GeneCards: SRF
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003131
NM_001292001

NM_020493

RefSeq (protein)

NP_001278930
NP_003122
NP_003122.1

NP_065239

Location (UCSC) Chr 6: 43.17 – 43.18 Mb Chr 17: 46.86 – 46.87 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Serum response factor, also known as SRF, is a transcription factor protein. [5]

Function

Serum response factor is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. [6] 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). [7] [8]

SRF is important during the development of the embryo, as it has been linked to the formation of mesoderm. [9] [10] In the fully developed mammal, SRF is crucial for the growth of skeletal muscle. [11] Interaction of SRF with other proteins, such as steroid hormone receptors, may contribute to regulation of muscle growth by steroids. [12] 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. [13]

Interactions

Serum response factor has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000112658Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000015605Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. S2CID  20004673.
  6. ^ 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.
  7. ^ 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. Bibcode: 1993RSPTB.340..325D. doi: 10.1098/rstb.1993.0074. PMID  8103935.
  8. ^ "SRF serum response factor". Entrez Gene. National Center for Biotechnology Information, National Institutes of Health.
  9. ^ 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.
  10. ^ Barron MR, Belaguli NS, Zhang SX, Trinh M, Iyer D, Merlo X, Lough JW, Parmacek MS, Bruneau BG, Schwartz RJ (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.
  11. ^ Li S, Czubryt MP, McAnally J, Bassel-Duby R, Richardson JA, Wiebel FF, Nordheim A, Olson EN (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. Bibcode: 2005PNAS..102.1082L. doi: 10.1073/pnas.0409103102. PMC  545866. PMID  15647354.
  12. ^ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ (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.
  13. ^ Koegel H, von Tobel L, Schäfer M, Alberti S, Kremmer E, Mauch C, Hohl D, Wang XJ, Beer HD, Bloch W, Nordheim A, Werner S (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.
  14. ^ Jung DJ, Sung HS, Goo YW, Lee HM, Park OK, Jung SY, Lim J, Kim HJ, Lee SK, Kim TS, Lee JW, Lee YC (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.
  15. ^ a b Zhu C, Johansen FE, Prywes R (September 1997). "Interaction of ATF6 and serum response factor". Mol. Cell. Biol. 17 (9): 4957–66. doi: 10.1128/MCB.17.9.4957. PMC  232347. PMID  9271374.
  16. ^ 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.
  17. ^ 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. doi: 10.1128/mcb.17.3.1744. PMC  231899. PMID  9032301.
  18. ^ a b Matsuzaki K, Minami T, Tojo M, Honda Y, Saitoh N, Nagahiro S, Saya H, Nakao M (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. S2CID  9697837.
  19. ^ 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.
  20. ^ 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.
  21. ^ 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.
  22. ^ 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. Bibcode: 1995Natur.373..632J. doi: 10.1038/373632a0. PMID  7854423. S2CID  47196160.
  23. ^ 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. doi: 10.1016/S0021-9258(17)41889-8. PMID  8106390.
  24. ^ Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL, Gilman M (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.
  25. ^ 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. doi: 10.1128/mcb.18.6.3310. PMC  108912. PMID  9584171.
  26. ^ Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D, Harel-Bellan A (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.
  27. ^ 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. doi: 10.1128/MCB.19.4.2577. PMC  84050. PMID  10082523.
  28. ^ 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. S2CID  28576187.
  29. ^ 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.
  30. ^ 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.
  31. ^ 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.

Further reading

External links

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