Disease relevance of POU6F2

• These data suggest that RPF-1 is likely to be involved in early steps in the differentiation of amacrine and ganglion cells [1].
• Purified RPF-1 was shown to bind to the adenovirus NF-1 binding site with high affinity [2].

High impact information on POU6F2

• Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors [3].
• Retina-derived POU-domain factor-1: a complex POU-domain gene implicated in the development of retinal ganglion and amacrine cells [1].
• In vitro, the RPF-1 POU domain lacking the insert binds to a consensus Oct-1 binding site, whereas the alternately spliced POU domain does not [1].
• In the adult, RPF-1 is expressed only within the CNS, where its expression is restricted to the medical habenulla, to a dispersed population of neurons in the dorsal hypothalamus, and to subsets of ganglion and amacrine cells in the retina [1].
• Nuclear import/export of hRPF1/Nedd4 regulates the ubiquitin-dependent degradation of its nuclear substrates [4].

Biological context of POU6F2

• Germline mutations of the POU6F2 gene in Wilms tumors with loss of heterozygosity on chromosome 7p14 [5].
• The only sequence shared by all six footprinted sequences is the trinucleotide, TGG, both of whose guanosines made contact with RPF-1, as determined by methylation interference assays [2].
• The footprinted sequence that binds RPF-1 with highest affinity contains the palindrome, TGG(N7)CCA, which conforms to the consensus sequence for binding NF-1, a nuclear protein that stimulates replication of adeno-virus-2 [2].

Other interactions of POU6F2

• No alteration of the WT1 and POU6F2 genes was identified in constitutional and tumor DNA of both sisters, and no anomaly in WT1 expression was evidenced in the normal kidney of one of them [6].
• Our search for nuclear substrates led to the identification of the human proline-rich transcript, brain-expressed (hPRTB) protein, the ubiquitination and degradation of which is regulated by hRPF1/Nedd4 [4].
• Finally, we demonstrate that hRPF1/Nedd4 is indeed capable of entering the nucleus; however, the presence of a functional Rev-like nuclear export sequence in hRPF1/Nedd4 ensures a predominant cytoplasmic localization [4].

References