Transcription factor Sp1

Definition:

Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component BMAL1. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity).

References:

[1]. Michelle R Bonello, et al. Fibroblast growth factor-2 represses platelet-derived growth factor receptor-alpha (PDGFR-alpha) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-alpha promoter. J Biol Chem. 2004 Jan 23;279(4):2377-82. [Content Brief]

[2]. Ying Zhang, et al. Phosphatidylinositol 3-kinase/protein kinase Czeta-induced phosphorylation of Sp1 and p107 repressor release have a critical role in histone deacetylase inhibitor-mediated derepression [corrected] of transcription of the luteinizing hormone receptor gene. Mol Cell Biol. 2006 Sep;26(18):6748-61. [Content Brief]

[3]. Sung Soo Chung, et al. Activation of PPARgamma negatively regulates O-GlcNAcylation of Sp1. Biochem Biophys Res Commun. 2008 Aug 8;372(4):713-8. [Content Brief]

[4]. Iwona Sachrajda, et al. Mithramycin A suppresses expression of the human melanoma-associated gene ABCB8. Mol Genet Genomics. 2011 Jan;285(1):57-65. [Content Brief]

[5]. Axel Vicart, et al. Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations. J Mol Biol. 2006 Dec 15;364(5):897-908. [Content Brief]

[6]. Beatrix A Olofsson, et al. Phosphorylation of Sp1 in response to DNA damage by ataxia telangiectasia-mutated kinase. Mol Cancer Res. 2007 Dec;5(12):1319-30. [Content Brief]

[7]. Ramona Jochmann, et al. O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter. J Virol. 2009 Apr;83(8):3704-18. [Content Brief]

[8]. Vittoria Infantino, et al. Identification of a novel Sp1 splice variant as a strong transcriptional activator. Biochem Biophys Res Commun. 2011 Aug 19;412(1):86-91. [Content Brief]

[9]. Mary L Spengler, et al. Phosphorylation mediates Sp1 coupled activities of proteolytic processing, desumoylation and degradation. Cell Cycle. 2008 Mar 1;7(5):623-30. [Content Brief]

[10]. X Yang, et al. O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6611-6. [Content Brief]

[11]. Jan-Jong Hung, et al. Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription. Mol Cell Biol. 2006 Mar;26(5):1770-85. [Content Brief]

[12]. Hoi-Tin Yu, et al. Transcriptional regulation of human FE65, a ligand of Alzheimer's disease amyloid precursor protein, by Sp1. J Cell Biochem. 2010 Mar 1;109(4):782-93. [Content Brief]

[13]. Ming-Chuan Hsu, et al. HER-2/neu represses the metastasis suppressor RECK via ERK and Sp transcription factors to promote cell invasion. J Biol Chem. 2006 Feb 24;281(8):4718-25. [Content Brief]

[14]. Jian-Ying Chuang, et al. Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the stability of transcription factor Sp1 during mitosis. Mol Biol Cell. 2008 Mar;19(3):1139-51. [Content Brief]

[15]. Satoko Iwahori, et al. Identification of phosphorylation sites on transcription factor Sp1 in response to DNA damage and its accumulation at damaged sites. Cell Signal. 2008 Oct;20(10):1795-803. [Content Brief]

[16]. H Ding, et al. Functional interactions between Sp1 or Sp3 and the helicase-like transcription factor mediate basal expression from the human plasminogen activator inhibitor-1 gene. J Biol Chem. 1999 Jul 9;274(28):19573-80. [Content Brief]

[17]. Julie Milanini-Mongiat, et al. Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelial growth factor gene transcription. J Biol Chem. 2002 Jun 7;277(23):20631-9. [Content Brief]

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