Abstract
KLF11 (Krüppel-like factor 11) belongs to the family of Sp1/Krüppel-like zinc finger transcription factors that play important roles in a variety of cell types and tissues. KLF11 was initially described as a transforming growth factor-beta (TGF-β) inducible immediate early gene (TIEG). KLF11 promotes the effects of TGF-β on cell growth control by influencing the TGFβ–Smads signaling pathway and regulating the transcription of genes that induce either apoptosis or cell cycle arrest. In carcinogenesis, KLF11 can show diverse effects. Its function as a tumor suppressor gene can be suppressed by phosphorylation of its binding domains via oncogenic pathways. However, KLF 11 can itself also show tumor-promoting effects and seems to have a crucial role in the epithelial–mesenchymal transition process. Here, we review the current knowledge about the function of KLF11 in cell growth regulation. We focus on its transcriptional regulatory function and its influence on the TGF-β signaling pathway. We further discuss its possible role in mediating crosstalk between various signaling pathways in normal cell growth and in carcinogenesis.
Highlights
The Krüppel protein regulates the body segmentation in the thorax and anterior abdomen of the Drosophila embryo in Drosophila melanogaster [1]
KLF11 promotes the effects of TGF-β on cell growth control by influencing the TGFβ–Smads signaling pathway and regulating the transcription of genes that induce either apoptosis or cell cycle arrest
KLF11 is hypermethylated in 15 % of myelodysplastic syndromes (MDS) cases, which is associated with a high International Prognostic Scoring System score
Summary
The Krüppel protein regulates the body segmentation in the thorax and anterior abdomen of the Drosophila embryo in Drosophila melanogaster [1]. The N-terminus contains the transcriptional regulatory domains that vary significantly It consists of acidic transactivation domains, Sin interacting domains (SID), or C-terminal binding protein (CtBP)-binding repressor domains that can bind co-factors and contribute to the distinct functions of KLFs [5]. TIEG1 and TIEG2 share several proline-rich sequences within the N-terminal domain, a property commonly found in other transcription factors as well [2,16,17,18,19,20] Both TIEG proteins, like all members of subgroup III, share in the N-terminus a conserved repression motif and an α-helical domain highly similar to the Sin interaction domain (SID) of the transcriptional repressor Mad1 [1]. We will focus on recent advances describing the different roles and mechanisms of KLF11 between normal cell growth and cell growth disorders, which is important for future analyzes regarding the role of KLF11 in carcinogenesis and which may lead to new insights and discoveries for cancer diagnosis or treatment
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