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Serum response factor

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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
Symbols  ; MCM1
External IDs GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Serum response factor (c-fos serum response element-binding transcription factor), also known as SRF, is a transcription factor.[1]

It 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 considered very 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.

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

Interactions

Serum response factor has been shown to interact with NFYA,[10] Src,[11] CREB-binding protein,[12] GTF2I,[13][14] ATF6,[15] Nuclear receptor co-repressor 2,[16] CEBPB,[17][18] GATA4,[19][20] Myogenin,[21][22] GTF2F1,[23][24] TEAD1,[25] ELK4,[15][26] Promyelocytic leukemia protein[12] and ASCC3.[27]

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.  
  2. ^ Shore P, Sharrocks AD (April 1995). "The MADS-box family of transcription factors". Eur. J. Biochem. 229 (1): 1–13.  
  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): 325–332.  
  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): 25775–25782.  
  6. ^ 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): 11816–11828.  
  7. ^ 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): 1082–1087.  
  8. ^ 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): 7786–7792.  
  9. ^ 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.  
  10. ^ Yamada, K; Osawa H; Granner D K (October 1999). "Identification of proteins that interact with NF-YA". FEBS Lett. (NETHERLANDS) 460 (1): 41–45.  
  11. ^ Kim, H J; Kim J H; Lee J W (October 1998). "Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations". J. Biol. Chem. (UNITED STATES) 273 (44): 28564–28567.  
  12. ^ a b Matsuzaki, Kazuhito; Minami Takeshi; Tojo Masahide; Honda Yoshiomi; Saitoh Noriko; Nagahiro Shinji; Saya Hideyuki; Nakao Mitsuyoshi (March 2003). "PML-nuclear bodies are involved in cellular serum response". Genes Cells (England) 8 (3): 275–286.  
  13. ^ Grueneberg, D A; Henry R W; Brauer A; Novina C D; Cheriyath V; Roy A L; 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. (UNITED STATES) 11 (19): 2482–2493.  
  14. ^ Kim, D W; Cheriyath V; Roy A L; Cochran B H (June 1998). "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Mol. Cell. Biol. (UNITED STATES) 18 (6): 3310–20.  
  15. ^ a b Zhu, C; Johansen F E; Prywes R (September 1997). "Interaction of ATF6 and serum response factor". Mol. Cell. Biol. (UNITED STATES) 17 (9): 4957–66.  
  16. ^ Lee, S K; Kim J H; Lee Y C; Cheong J; Lee J W (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. (UNITED STATES) 275 (17): 12470–12474.  
  17. ^ Hanlon, M; Sealy L (May 1999). "Ras regulates the association of serum response factor and CCAAT/enhancer-binding protein beta". J. Biol. Chem. (UNITED STATES) 274 (20): 14224–14228.  
  18. ^ Sealy, L; Malone D; Pawlak M (March 1997). "Regulation of the cfos serum response element by C/EBPbeta". Mol. Cell. Biol. (UNITED STATES) 17 (3): 1744–55.  
  19. ^ Belaguli, N S; Sepulveda J L; Nigam V; Charron F; Nemer M; Schwartz R J (October 2000). "Cardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulators". Mol. Cell. Biol. (UNITED STATES) 20 (20): 7550–7558.  
  20. ^ 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. (United States) 21 (4): 1036–1044.  
  21. ^ Groisman, R; Masutani H; Leibovitch M P; 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. (UNITED STATES) 271 (9): 5258–5264.  
  22. ^ 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. (UNITED STATES) 19 (4): 2577–84.  
  23. ^ Joliot, V; Demma M; Prywes R (February 1995). "Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor".  
  24. ^ Zhu, H; Joliot V; Prywes R (February 1994). "Role of transcription factor TFIIF in serum response factor-activated transcription". J. Biol. Chem. (UNITED STATES) 269 (5): 3489–97.  
  25. ^ Gupta, M; Kogut P; Davis F J; Belaguli N S; Schwartz R J; Gupta M P (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. (United States) 276 (13): 10413–10422.  
  26. ^ Hassler, M; Richmond T J (June 2001). "The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex". EMBO J. (England) 20 (12): 3018–3028.  
  27. ^ Jung, Dong-Ju; Sung Hee-Sook, Goo Young-Wha, Lee Hyun Mi, Park Ok Ku, Jung Sung-Yun, Lim Janghoo, Kim Han-Jong, Lee Soo-Kyung, Kim Tae Sung, Lee Jae Woon, Lee Young Chul (July 2002). "Novel transcription coactivator complex containing activating signal cointegrator 1". Mol. Cell. Biol. (United States) 22 (14): 5203–5211.  

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