Serum response factor

Serum response factor, also known as SRF, is a transcription factor protein.{{cite journal | vauthors = Norman C, Runswick M, Pollock R, Treisman R | title = Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element | journal = Cell | volume = 55 | issue = 6 | pages = 989–1003 | date = December 1988 | pmid = 3203386 | doi = 10.1016/0092-8674(88)90244-9 | s2cid = 20004673 }}

Function

Serum response factor is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors.{{cite journal | vauthors = Shore P, Sharrocks AD | title = The MADS-box family of transcription factors | journal = Eur. J. Biochem. | volume = 229 | issue = 1 | pages = 1–13 | date = April 1995 | pmid = 7744019 | doi = 10.1111/j.1432-1033.1995.0001l.x }} 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).{{cite journal | vauthors = Dalton S, Marais R, Wynne J, Treisman R | title = Isolation and characterization of SRF accessory proteins | journal = Philos. Trans. R. Soc. Lond. B Biol. Sci. | volume = 340 | issue = 1293 | pages = 325–32 | date = June 1993 | pmid = 8103935 | doi = 10.1098/rstb.1993.0074 | bibcode = 1993RSPTB.340..325D }}{{cite web | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6722 | title = SRF serum response factor | work = Entrez Gene | publisher = National Center for Biotechnology Information, National Institutes of Health}}

SRF is important during the development of the embryo, as it has been linked to the formation of mesoderm.{{cite journal | vauthors = Sepulveda JL, Vlahopoulos S, Iyer D, Belaguli N, Schwartz RJ | title = Combinatorial expression of GATA4, Nkx2-5, and serum response factor directs early cardiac gene activity | journal = J. Biol. Chem. | volume = 277 | issue = 28 | pages = 25775–82 | date = July 2002 | pmid = 11983708 | doi = 10.1074/jbc.M203122200 | doi-access = free }}{{cite journal | vauthors = Barron MR, Belaguli NS, Zhang SX, Trinh M, Iyer D, Merlo X, Lough JW, Parmacek MS, Bruneau BG, Schwartz RJ | title = Serum response factor, an enriched cardiac mesoderm obligatory factor, is a downstream gene target for Tbx genes | journal = J. Biol. Chem. | volume = 280 | issue = 12 | pages = 11816–28 | date = March 2005 | pmid = 15591049 | doi = 10.1074/jbc.M412408200 | doi-access = free }} In the fully developed mammal, SRF is crucial for the growth of skeletal muscle.{{cite journal | vauthors = Li S, Czubryt MP, McAnally J, Bassel-Duby R, Richardson JA, Wiebel FF, Nordheim A, Olson EN | title = Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | issue = 4 | pages = 1082–7 | date = January 2005 | pmid = 15647354 | pmc = 545866 | doi = 10.1073/pnas.0409103102 | bibcode = 2005PNAS..102.1082L | doi-access = free }} Interaction of SRF with other proteins, such as steroid hormone receptors, may contribute to regulation of muscle growth by steroids.{{cite journal | vauthors = Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ | title = Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene | journal = J. Biol. Chem. | volume = 280 | issue = 9 | pages = 7786–92 | date = March 2005 | pmid = 15623502 | doi = 10.1074/jbc.M413992200 | doi-access = free }} 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.{{cite journal | vauthors = 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 | title = Loss of serum response factor in keratinocytes results in hyperproliferative skin disease in mice | journal = J. Clin. Invest. | volume = 119 | issue = 4 | pages = 899–910 | date = April 2009 | pmid = 19307725 | pmc = 2662566 | doi = 10.1172/JCI37771 }}

Interactions

Serum response factor has been shown to interact with:

ASCC3,{{cite journal | vauthors = Jung DJ, Sung HS, Goo YW, Lee HM, Park OK, Jung SY, Lim J, Kim HJ, Lee SK, Kim TS, Lee JW, Lee YC | title = Novel transcription coactivator complex containing activating signal cointegrator 1 | journal = Mol. Cell. Biol. | volume = 22 | issue = 14 | pages = 5203–11 | date = July 2002 | pmid = 12077347 | pmc = 139772 | doi = 10.1128/mcb.22.14.5203-5211.2002}}
ATF6,{{cite journal | vauthors = Zhu C, Johansen FE, Prywes R | title = Interaction of ATF6 and serum response factor | journal = Mol. Cell. Biol. | volume = 17 | issue = 9 | pages = 4957–66 | date = September 1997 | pmid = 9271374 | pmc = 232347 | doi = 10.1128/MCB.17.9.4957}}
CEBPB,{{cite journal | vauthors = Hanlon M, Sealy L | title = Ras regulates the association of serum response factor and CCAAT/enhancer-binding protein beta | journal = J. Biol. Chem. | volume = 274 | issue = 20 | pages = 14224–8 | date = May 1999 | pmid = 10318842 | doi = 10.1074/jbc.274.20.14224| doi-access = free }}{{cite journal | vauthors = Sealy L, Malone D, Pawlak M | title = Regulation of the cfos serum response element by C/EBPbeta | journal = Mol. Cell. Biol. | volume = 17 | issue = 3 | pages = 1744–55 | date = March 1997 | pmid = 9032301 | pmc = 231899 | doi = 10.1128/mcb.17.3.1744}}
CREB-binding protein,{{cite journal | vauthors = Matsuzaki K, Minami T, Tojo M, Honda Y, Saitoh N, Nagahiro S, Saya H, Nakao M | title = PML-nuclear bodies are involved in cellular serum response | journal = Genes Cells | volume = 8 | issue = 3 | pages = 275–86 | date = March 2003 | pmid = 12622724 | doi = 10.1046/j.1365-2443.2003.00632.x| s2cid = 9697837 | doi-access = free }}
ELK4,{{cite journal | vauthors = Hassler M, Richmond TJ | title = The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex | journal = EMBO J. | volume = 20 | issue = 12 | pages = 3018–28 | date = June 2001 | pmid = 11406578 | pmc = 150215 | doi = 10.1093/emboj/20.12.3018 }}
GATA4,{{cite journal | vauthors = Belaguli NS, Sepulveda JL, Nigam V, Charron F, Nemer M, Schwartz RJ | title = Cardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulators | journal = Mol. Cell. Biol. | volume = 20 | issue = 20 | pages = 7550–8 | date = October 2000 | pmid = 11003651 | pmc = 86307 | doi = 10.1128/mcb.20.20.7550-7558.2000}}{{cite journal | vauthors = Morin S, Paradis P, Aries A, Nemer M | title = Serum response factor-GATA ternary complex required for nuclear signaling by a G-protein-coupled receptor | journal = Mol. Cell. Biol. | volume = 21 | issue = 4 | pages = 1036–44 | date = February 2001 | pmid = 11158291 | pmc = 99558 | doi = 10.1128/MCB.21.4.1036-1044.2001 }}
GTF2F1,{{cite journal | vauthors = Joliot V, Demma M, Prywes R | title = Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor | journal = Nature | volume = 373 | issue = 6515 | pages = 632–5 | date = February 1995 | pmid = 7854423 | doi = 10.1038/373632a0 | bibcode = 1995Natur.373..632J | s2cid = 47196160 }}{{cite journal | vauthors = Zhu H, Joliot V, Prywes R | title = Role of transcription factor TFIIF in serum response factor-activated transcription | journal = J. Biol. Chem. | volume = 269 | issue = 5 | pages = 3489–97 | date = February 1994 | doi = 10.1016/S0021-9258(17)41889-8 | pmid = 8106390 | doi-access = free }}
GTF2I,{{cite journal | vauthors = Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL, Gilman M | title = A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I | journal = Genes Dev. | volume = 11 | issue = 19 | pages = 2482–93 | date = October 1997 | pmid = 9334314 | pmc = 316568 | doi = 10.1101/gad.11.19.2482}}{{cite journal | vauthors = Kim DW, Cheriyath V, Roy AL, Cochran BH | title = TFII-I enhances activation of the c-fos promoter through interactions with upstream elements | journal = Mol. Cell. Biol. | volume = 18 | issue = 6 | pages = 3310–20 | date = June 1998 | pmid = 9584171 | pmc = 108912 | doi = 10.1128/mcb.18.6.3310}}
Myogenin,{{cite journal | vauthors = Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D, Harel-Bellan A | title = Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins | journal = J. Biol. Chem. | volume = 271 | issue = 9 | pages = 5258–64 | date = March 1996 | pmid = 8617811 | doi = 10.1074/jbc.271.9.5258| doi-access = free }}{{cite journal | vauthors = Biesiada E, Hamamori Y, Kedes L, Sartorelli V | title = 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 | journal = Mol. Cell. Biol. | volume = 19 | issue = 4 | pages = 2577–84 | date = April 1999 | pmid = 10082523 | pmc = 84050 | doi = 10.1128/MCB.19.4.2577}}
NFYA,{{cite journal | vauthors = Yamada K, Osawa H, Granner DK | title = Identification of proteins that interact with NF-YA | journal = FEBS Lett. | volume = 460 | issue = 1 | pages = 41–5 | date = October 1999 | pmid = 10571058 | doi = 10.1016/s0014-5793(99)01311-3| s2cid = 28576187 | doi-access = free | bibcode = 1999FEBSL.460...41Y }}
Nuclear receptor co-repressor 2,{{cite journal | vauthors = Lee SK, Kim JH, Lee YC, Cheong J, Lee JW | title = 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 | journal = J. Biol. Chem. | volume = 275 | issue = 17 | pages = 12470–4 | date = April 2000 | pmid = 10777532 | doi = 10.1074/jbc.275.17.12470| doi-access = free }}
Promyelocytic leukemia protein and
Src,{{cite journal | vauthors = Kim HJ, Kim JH, Lee JW | title = Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations | journal = J. Biol. Chem. | volume = 273 | issue = 44 | pages = 28564–7 | date = October 1998 | pmid = 9786846 | doi = 10.1074/jbc.273.44.28564| doi-access = free }} and
TEAD1.{{cite journal | vauthors = Gupta M, Kogut P, Davis FJ, Belaguli NS, Schwartz RJ, Gupta MP | title = Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1 | journal = J. Biol. Chem. | volume = 276 | issue = 13 | pages = 10413–22 | date = March 2001 | pmid = 11136726 | doi = 10.1074/jbc.M008625200 | doi-access = free }}

References

External links

{{MeshName|Serum+Response+Factor}}
{{FactorBook|SRF}}

{{NLM content|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6722}}

Category:Transcription factors