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Journal of Neuroscience, Vol 16, 2261-2274, Copyright © 1996 by Society for Neuroscience
Retina-derived POU-domain factor-1: a complex POU-domain gene implicated in the development of retinal ganglion and amacrine cells
H Zhou, T Yoshioka and J Nathans
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
A novel POU-domain protein, retina-derived POU-domain factor-1 (RPF-1), has
been identified through the isolation of cDNA and genomic DNA clones. 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. The human RPF-1 gene spans > 125 kb and gives rise to
multiple differentially spliced transcripts. In the human retina, the most
abundant mRNA isoforms are derived from an alternate splicing event that
inserts an evolutionarily conserved peptide of 36 amino acids into the DNA
recognition helix of the POU- specific domain. 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. RPF-1 protein first appears in
the developing mouse retina at e11, where it localizes to neuroblasts that
have recently migrated from the mitotic zone to the future ganglion cell
layer. These data suggest that RPF-1 is likely to be involved in early
steps in the differentiation of amacrine and ganglion cells.
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