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- Table of Contents
Facts about Krueppel-like factor 8.
Also binds the GT-box of cyclin D1 promoter and mediates cell cycle progression at G(1) phase as a downstream target of focal adhesion kinase (FAK). .
Human | |
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Gene Name: | KLF8 |
Uniprot: | O95600 |
Entrez: | 11279 |
Belongs to: |
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Sp1 C2H2-type zinc-finger protein family |
Basic krueppel-like factor 3; basic kruppel-like factor 3; BKLF3DKFZp686O08126; DXS741; Krueppel-like factor 8; Kruppel-like factor 8; Zinc finger protein 741; ZNF741MGC138314
Mass (kDA):
39.314 kDA
Human | |
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Location: | Xp11.21 |
Sequence: | X; NC_000023.11 (55908123..56291531) |
Ubiquitous.
Nucleus.
The KLF8 indicator is a nuclear localization signal. It features a CACCC box, and a valinerich hydrophobic stretch. It allows scientists to analyze their results and submit them for species, applications, as well as other purposes. The product credits given are applicable to scientists all over the world, so anyone can use this marker. To learn more about the KLF8 marker, keep reading.
Despite the high homology between the two KLF proteins, they contribute to nuclear localization differently. Their respective nuclear "traffic signal" signals are not identical. This may be a reason for their different functions. Mehta et al. Mehta and colleagues discovered a functional NLS to KLF8 in the ZF domain. They concluded it is necessary for nuclear localization.
Previous sequence homology analyses have identified two possible NLSs within KLF8. The first NLS can be found upstream of two zinc fingers while the second can be found at the carboxy end of the protein sequence. In previous experiments, we had found that the NLSs were not necessary for nuclear localization, but rather merely served to stabilize the localization of the protein. Mutation of one of the NLSs did not change the nuclear localization of the protein.
Mutations in one of these aminos or both can result in a decrease of downstream NLS expression. Both of these amino acids are required for KLF8 to up-regulate the expression of cyclin D1; mutations in either S165 or K171 reduce cyclin D1 promoter induction. These mutations also decrease cellular proliferation. KLF8 is an excellent candidate to test for nuclear localization.
The mutation of KLF8's nucleoplasmic nuclear fusion protein results the phosphorylation and activation of the nonNLS sequence. The non-NLS sequence could also play an important part in maintaining NLS function and inhibiting nuclear export of this protein. Additional experiments are required to determine whether this sequence inhibits nuclear export of the protein. A final important question is whether or not this sequence regulates the interaction between nuclear importin and exportin.
The role of nuclear localization signal (NLS) is complex. It contributes to the development of novel antiviral medicines and therapeutic vaccines. NLSs are expressed by different cell types and must be explored in detail to identify which proteins they bind. Understanding how NLSs are translocated through the NPC is a major challenge for the future. This research is expected help us understand the role nuclear localization signals play when developing novel therapeutic vaccines or other antiviral medications.
The BI-NP–NLS–MxBD(1-25) mutation demonstrated that MxBlocalizes within the nuclear envelope. Importin-b is a prerequisite for MxB's NTS. Cells were transfected with wild type MxB and truncated mxB to visualize the subcellular locations of MxB. Confocal laser scanning microscopy (FLSM) was used to observe its subcellular localization in HeLa cells.
The KLF8 family gene is located on chromosomes 19, 22 and 23. It is the most prevalent member of the group. KLF8 binds with the CACCC Box in the human genome, and has a high affinity for GC-boxes. It can also bind to a CACCCbox, which is rarer for other transcription factors. This is an exciting discovery, but more research is needed to confirm it.
Various studies have indicated that KLF8 expression in gastric cancer is associated with poor prognosis. KLF8 is a key component of gastric cancer. It can be silenced by targeting GLUT4 - which is a CACCCbox. KLF8 may be a new biomarker to help this type of cancer survive and possibly a therapeutic target.
17 members make up the KLF family. They all play a key role in controlling various cell types' biological functions. Most of them recognize a CACCC-box element and function as transcriptional activators or repressors. The regulation of gastric carcinoma is affected by several members. They function by binding to specific target genes, thereby inducing or suppressing their expression.
In a previous study it was found that the KLF8 genes binds to a CACCC box. A KLF8-specific bindin was also observed in the promoter area of cyclin E1. KLF8 can activate the target cyclin D1 by binding to the GT sequence.
Mutations in this critical consensus binding site will cause the gene to cease being able to form the shift-band. Complex formation can be prevented by mutants in the gene by using unlabeled GT Box A oligonucleotides. Furthermore, competition experiments show that the unlabeled GT box A oligonucleotide inhibits complex formation, and nuclear extracts from induced cells abolish the ability of the mutant to form the complex. The complex formation could also be completely abated by including anti-KLF8 antigens.
Although the KLF8Marker can bind directly to the CACCCbox, there are many other factors that can bind CAC boxes. Sp1 is one example. Some researchers suggest that EKLF may bind the CAC box of globin gene promoter, activating transcription in vitro. The KLF8Marker has also been shown to regulate transcription in hematopoietic tissue.
KLF8 regulates GLUT4 mRNA. Knockdown of KLF8 decreased GLUT4 mRNA in AGS cells. Immunofluorescence and Western blot analysis confirmed the knockdown of KLF8. Further, KLF8 has a role in regulating GLUT4 in a tumor-associated mouse model.
The KLF8 genome encodes a protein that contains 359 amino acids and is required for nucleotide attachment. The sequence of this gene predicts a valine-rich hydrophobic stretch and a nuclear localization signal upstream of zinc fingers. The KLF8 protein interacts with CTBP2 through a PVDLS pattern.
PMID: 23134681 by Camacho-Vanegas O., et al. Shaking the family tree: Identification of novel and biologically active alternatively spliced isoforms across the KLF family of transcription factors.
PMID: 10756197 by van Vliet J., et al. Human Kruppel-like factor 8: a CACCC-box binding protein that associates with CtBP and represses transcription.