Disease relevance of Cutl2

• The expression of the Cux2 protein was convincingly detected in only one among 19 neuronal cell lines: the SH-SY5Y human neuroblastoma cell line [1].

High impact information on Cutl2

• Unlike Cux-1, expression of Cux-2 was restricted to neural tissue [2].
• The murine Cux-2 homeobox was similar to Drosophila cut and encoded a homeodomain that contained a characteristic histidine residue at position 50 [2].
• Cux-2 is expressed exclusively in the central and peripheral nervous systems, and the Cux-2 gene product binds to DNA in a sequence-specific manner [2].
• In the adult brain, Cux-2 was prominently expressed in neurons in the thalamus and limbic system [2].
• In embryos, Cux-2 was expressed in the developing central and peripheral nervous systems, including the telencephalon and peripheral ganglia of the trigeminal and glossopharyngeal nerves [2].

Biological context of Cutl2

• More recently, vertebrates were found to possess a second cut orthologs that was generated by gene duplication: Cux2 [1].
• Here we describe the dynamic profile of Cux2 during mouse embryogenesis [3].
• Cux2 is hypothesized to function as a transcriptional regulator that inhibits terminal differentiation and cell cycle exit [3].
• Cux2 expression coincides with many tissue regions undergoing proliferative growth or cell rearrangements, however some later expression domains also include sites of programmed cell death [3].

Anatomical context of Cutl2

• Expression of Cux-1 and Cux-2 in the subventricular zone and upper layers II-IV of the cerebral cortex [4].
• Expression of Cux-1 and Cux-2 in the developing somatosensory cortex of normal and barrel-defective mice [5].

Associations of Cutl2 with chemical compounds

• Cux-2 mRNA expression is also found in the embryonic SVZ, overlapping with BrdU-positive dividing precursors, but it is not expressed in the VZ [4].

Physical interactions of Cutl2

• Mechanistically, we discovered through chromatin immunoprecipitation assays that Cux2 binds both the Neurod and p27(Kip1) promoters in vivo, indicating that these interactions are direct [6].

Other interactions of Cutl2

• We did not observe an N-terminally processed Cux2 isoform equivalent to the Cux1 p110 isoform [1].
• Using different molecular markers and Pax6-deficient mice, we provide data that suggest a relationship between the early-determined Cux2-positive neuronal precursors in the SVZ/IZ and upper layer neurons [7].
• Dynamic expression of murine Cux2 in craniofacial, limb, urogenital and neuronal primordia [3].
• Our findings suggest that Cux2 might mediate some of the effects of Notch signaling on interneuron formation [8].

References