Limits...
The CSL proteins, versatile transcription factors and context dependent corepressors of the notch signaling pathway

View Article: PubMed Central - PubMed

ABSTRACT

The Notch signaling pathway is a reiteratively used cell to cell communication pathway that triggers pleiotropic effects. The correct regulation of the pathway permits the efficient regulation of genes involved in cell fate decision throughout development. This activity relies notably on the CSL proteins, (an acronym for CBF-1/RBPJ-κ in Homo sapiens/Mus musculus respectively, Suppressor of Hairless in Drosophila melanogaster, Lag-1 in Caenorhabditis elegans) which is the unique transcription factor and DNA binding protein involved in this pathway. The CSL proteins have the capacity to recruit activation or repression complexes according to the cellular context. The aim of this review is to describe the different co-repressor proteins that interact directly with CSL proteins to form repression complexes thereby regulating the Notch signaling pathway in animal cells to give insights into the paralogous evolution of these co-repressors in higher eumetazoans and their subsequent effects at developmental processes.

No MeSH data available.


RITA-CSL. This interaction represents a different, but still important mechanism of regulation of the NSP. In this case chromatin modification is not involved, instead the complex is shuttle out of the nucleus by activity of RITA. The CSL interacting domain with RITA is mapped at the CTD
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

License 1 - License 2
getmorefigures.php?uid=PMC5037638&req=5

Fig7: RITA-CSL. This interaction represents a different, but still important mechanism of regulation of the NSP. In this case chromatin modification is not involved, instead the complex is shuttle out of the nucleus by activity of RITA. The CSL interacting domain with RITA is mapped at the CTD

Mentions: The RBPJ-κ interacting and tubulin associated protein (RITA) was identify and characterized by Wacker et al. [98]. The 36 kDa RITA protein contains a tubulin interaction domain, a functional nuclear localization signal (NLS), a nuclear export signal (NES), and the RBP-J-interaction domain at the central region of the protein. These domains are used by RITA to interact with nuclear RBPJ-κ protein and to shuttle the transcription factor out of the nucleus, negatively regulating the Notch signaling pathway in vertebrates such as Xenopus laevis and the mouse [98]. Brockmann et al. [99] analyzed the Su(H) interaction capacity and effects of ectopically expressed RITA in Drosophila, where no RITA-homologue has been detected in the genome. In those experiments they demonstrated that RITA interacts with the C-terminal domain of the Su(H) (Fig. 7) in vitro and in vivo, even though overexpression of RITA in Drosophila had not significant phenotypic effects [99].Fig. 7


The CSL proteins, versatile transcription factors and context dependent corepressors of the notch signaling pathway
RITA-CSL. This interaction represents a different, but still important mechanism of regulation of the NSP. In this case chromatin modification is not involved, instead the complex is shuttle out of the nucleus by activity of RITA. The CSL interacting domain with RITA is mapped at the CTD
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC5037638&req=5

Fig7: RITA-CSL. This interaction represents a different, but still important mechanism of regulation of the NSP. In this case chromatin modification is not involved, instead the complex is shuttle out of the nucleus by activity of RITA. The CSL interacting domain with RITA is mapped at the CTD
Mentions: The RBPJ-κ interacting and tubulin associated protein (RITA) was identify and characterized by Wacker et al. [98]. The 36 kDa RITA protein contains a tubulin interaction domain, a functional nuclear localization signal (NLS), a nuclear export signal (NES), and the RBP-J-interaction domain at the central region of the protein. These domains are used by RITA to interact with nuclear RBPJ-κ protein and to shuttle the transcription factor out of the nucleus, negatively regulating the Notch signaling pathway in vertebrates such as Xenopus laevis and the mouse [98]. Brockmann et al. [99] analyzed the Su(H) interaction capacity and effects of ectopically expressed RITA in Drosophila, where no RITA-homologue has been detected in the genome. In those experiments they demonstrated that RITA interacts with the C-terminal domain of the Su(H) (Fig. 7) in vitro and in vivo, even though overexpression of RITA in Drosophila had not significant phenotypic effects [99].Fig. 7

View Article: PubMed Central - PubMed

ABSTRACT

The Notch signaling pathway is a reiteratively used cell to cell communication pathway that triggers pleiotropic effects. The correct regulation of the pathway permits the efficient regulation of genes involved in cell fate decision throughout development. This activity relies notably on the CSL proteins, (an acronym for CBF-1/RBPJ-κ in Homo sapiens/Mus musculus respectively, Suppressor of Hairless in Drosophila melanogaster, Lag-1 in Caenorhabditis elegans) which is the unique transcription factor and DNA binding protein involved in this pathway. The CSL proteins have the capacity to recruit activation or repression complexes according to the cellular context. The aim of this review is to describe the different co-repressor proteins that interact directly with CSL proteins to form repression complexes thereby regulating the Notch signaling pathway in animal cells to give insights into the paralogous evolution of these co-repressors in higher eumetazoans and their subsequent effects at developmental processes.

No MeSH data available.