Wolf, Dorina B. published the artcileNucleo-cytoplasmic shuttling of murine RBPJ by Hairless protein matches that of Su(H) protein in the model system Drosophila melanogaster, Synthetic Route of 59-23-4, the main research area is murine protein nucleocytoplasmic shuttling Drosophila melanogaster; CBF1; Drosophila; Hairless, CSL; Notch signal transduction; Nucleo-cytoplasmic transport; Protein availability; RPBJ; Su(H); Transcription repression.
CSL transcription factors are central to signal transduction in the highly conserved Notch signaling pathway. CSL acts as a mol. switch: depending on the cofactors recruited, CSL induces either activation or repression of Notch target genes. Unexpectedly, CSL depends on its cofactors for nuclear entry, despite its role as gene regulator. In Drosophila, the CSL homolog Suppressor of Hairless (Su(H)), recruits Hairless (H) for repressor complex assembly, and eventually for nuclear import. We recently found that Su(H) is subjected to a dynamic nucleo-cytoplasmic shuttling, thereby strictly following H subcellular distribution. Hence, regulation of nuclear availability of Su(H) by H may represent a new layer of control of Notch signaling activity. Here we extended this work on the murine CSL homolog RBPJ. Using a ‘murinized’ fly model bearing RBPJwt in place of Su(H) at the endogenous locus we demonstrate that RBPJ protein likewise follows H subcellular distribution. For example, overexpression of a H*NLS3 protein variant defective of nuclear import resulted in a cytosolic localization of RBPJ protein, whereas the overexpression of a H*NES protein variant defective in the nuclear export signal caused the accumulation of RBPJ protein in the nucleus. Evidently, RBPJ is exported from the nucleus as well. Overall these data demonstrate that in our fly model, RBPJ is subjected to H-mediated nucleo-cytoplasmic shuttling as is Su(H). These data raise the possibility that nuclear availability of mammalian CSL proteins is likewise restricted by cofactors, and may hence present a more general mode of regulating Notch signaling activity.
Hereditas (London, United Kingdom) published new progress about Cytoplasm. 59-23-4 belongs to class alcohols-buliding-blocks, name is (2R,3S,4S,5R)-2,3,4,5,6-Pentahydroxyhexanal, and the molecular formula is C6H12O6, Synthetic Route of 59-23-4.
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