Limits...
Transcriptional regulation of metastatic [Id]entity by KLF17.

Iwanicki MP, Brugge JS - Genome Biol. (2009)

Bottom Line: A novel in vivo screening approach has identified KLF17 as a key metastasis suppressor gene that acts through regulation of Id1 transcription factor-dependent induction of the epithelial-to-mesenchymal transition.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

ABSTRACT
A novel in vivo screening approach has identified KLF17 as a key metastasis suppressor gene that acts through regulation of Id1 transcription factor-dependent induction of the epithelial-to-mesenchymal transition.

Show MeSH

Related in: MedlinePlus

Regulation of ID1 expression by KLF17. ID1 transcription is suppressed by KLF17 binding to the ID1 promoter. Loss of expression of KLF17 by transcriptional suppression or inactivation by post-translational modification (possibly by phosphorylation or dephosphorylation) leads to transcription of ID1 through positive transcriptional regulators (shown in green) and induction of the multiple processes regulated by its protein product, Id1.
© Copyright Policy
Related In: Results  -  Collection


getmorefigures.php?uid=PMC3091312&req=5

Figure 1: Regulation of ID1 expression by KLF17. ID1 transcription is suppressed by KLF17 binding to the ID1 promoter. Loss of expression of KLF17 by transcriptional suppression or inactivation by post-translational modification (possibly by phosphorylation or dephosphorylation) leads to transcription of ID1 through positive transcriptional regulators (shown in green) and induction of the multiple processes regulated by its protein product, Id1.

Mentions: One important question raised by the work of Gumireddy et al. [3] is whether the regulation of KLF17 is entirely transcriptional or if its activity is also regulated post-translationally, and what upstream factors control gene expression or protein activity. The transcriptional activity of Sp1/KLF family members has been shown to be regulated post-translationally by phosphorylation [8,22]. A search for phosphorylation-site motifs using Scansite [23] predicts a high-stringency target site for phosphorylation by protein kinase C-ε (PKCε) within the amino-terminal region of KLF17. Given that the activity of some Sp1/KLF family members is known to be regulated by PKC isoforms [8,24-26], it is plausible that the ability of KLF17 to suppress ID1 transcription could be either positively or negatively tuned by some PKCs (Figure 1). However, future experiments addressing the mechanisms of KLF17 regulation will be needed to fill this gap in our understanding of metastatic progression.


Transcriptional regulation of metastatic [Id]entity by KLF17.

Iwanicki MP, Brugge JS - Genome Biol. (2009)

Regulation of ID1 expression by KLF17. ID1 transcription is suppressed by KLF17 binding to the ID1 promoter. Loss of expression of KLF17 by transcriptional suppression or inactivation by post-translational modification (possibly by phosphorylation or dephosphorylation) leads to transcription of ID1 through positive transcriptional regulators (shown in green) and induction of the multiple processes regulated by its protein product, Id1.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3091312&req=5

Figure 1: Regulation of ID1 expression by KLF17. ID1 transcription is suppressed by KLF17 binding to the ID1 promoter. Loss of expression of KLF17 by transcriptional suppression or inactivation by post-translational modification (possibly by phosphorylation or dephosphorylation) leads to transcription of ID1 through positive transcriptional regulators (shown in green) and induction of the multiple processes regulated by its protein product, Id1.
Mentions: One important question raised by the work of Gumireddy et al. [3] is whether the regulation of KLF17 is entirely transcriptional or if its activity is also regulated post-translationally, and what upstream factors control gene expression or protein activity. The transcriptional activity of Sp1/KLF family members has been shown to be regulated post-translationally by phosphorylation [8,22]. A search for phosphorylation-site motifs using Scansite [23] predicts a high-stringency target site for phosphorylation by protein kinase C-ε (PKCε) within the amino-terminal region of KLF17. Given that the activity of some Sp1/KLF family members is known to be regulated by PKC isoforms [8,24-26], it is plausible that the ability of KLF17 to suppress ID1 transcription could be either positively or negatively tuned by some PKCs (Figure 1). However, future experiments addressing the mechanisms of KLF17 regulation will be needed to fill this gap in our understanding of metastatic progression.

Bottom Line: A novel in vivo screening approach has identified KLF17 as a key metastasis suppressor gene that acts through regulation of Id1 transcription factor-dependent induction of the epithelial-to-mesenchymal transition.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

ABSTRACT
A novel in vivo screening approach has identified KLF17 as a key metastasis suppressor gene that acts through regulation of Id1 transcription factor-dependent induction of the epithelial-to-mesenchymal transition.

Show MeSH
Related in: MedlinePlus