TY - JOUR
T1 - Retina-derived POU-domain factor-1
T2 - A complex POU-domain gene implicated in the development of retinal ganglion and amacrine cells
AU - Zhou, Hao
AU - Yoshioka, Takashi
AU - Nathans, Jeremy
PY - 1996/4/1
Y1 - 1996/4/1
N2 - 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 medial 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.
AB - 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 medial 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.
KW - POU domain
KW - RPF- 1
KW - amacrine cells
KW - retina
KW - retinal ganglion cells
KW - transcription factor
UR - http://www.scopus.com/inward/record.url?scp=0029992185&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029992185&partnerID=8YFLogxK
U2 - 10.1523/jneurosci.16-07-02261.1996
DO - 10.1523/jneurosci.16-07-02261.1996
M3 - Article
C2 - 8601806
AN - SCOPUS:0029992185
SN - 0270-6474
VL - 16
SP - 2261
EP - 2274
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 7
ER -