?
N-terminal domain of Kruppel-like factor 8 Kruppel-like factor 8 (also known as Krueppel-like transcription factor 8, KLF8) is a CACCC-box binding protein that associates with C-terminal Binding Protein (CtBP) and represses transcription. It plays an essential role in the regulation of the cell cycle, apoptosis, and differentiation. It has been identified as a key component of the transcription factor network that controls terminal differentiation during adipogenesis. It also plays an important role in the formation of several human tumors, including the promotion of tumorigenesis, invasion, and metastasis of colorectal cancer cells, and the progression of pancreatic cancer. KLF8 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. KLF8 contains an N-terminal repression domain that is related to that of KLF12.
|