Role of a transcription factor Pax6 in the developing vertebrate olfactory system

Nomura, Tadashi; Haba, Hasumi; Osumi, Noriko

doi:10.1111/j.1440-169x.2007.00965.x

Cited by 48 publications

(32 citation statements)

References 75 publications

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“…lens, retina, cornea, iris, olfactory epithelium, forebrain, cerebellum, and pancreas) (41,43,44,79). It has been shown that Pax6 regulates the batteries of common target genes in distinct tissues, including the lens and neurons (57,80).…”

Section: Discussionmentioning

confidence: 99%

“…Thus, in contrast to the majority of sequencespecific DNA binding proteins that use a single DNA-binding domain that typically docks with 6 -10 bp of DNA, Pax6 can use ␤-sheets, PAI, linker, RED, and HD, and their various combinations to bind DNA. Although some important direct targets of Pax6 genes have been identified (41), a large body of work remains to be accomplished (42)(43)(44). Some transcription factors, especially those with multiple DNA-binding subdomains (e.g.…”

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confidence: 99%

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The Orchestration of Mammalian Tissue Morphogenesis through a Series of Coherent Feed-forward Loops

Xie

Cvekl

2011

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

The Orchestration of Mammalian Tissue Morphogenesis through a Series of Coherent Feed-forward Loops

Xie

Cvekl

2011

Journal of Biological Chemistry

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“…The transcription factor Pax6 is highly conserved among vertebrates and is essential for a wide variety of developmental processes within the central nervous system (CNS), sensory organs, and the endocrine system [15][16][17][18][19]. Homozygous Pax6 mutant mice (Pax6…”

Section: Introductionmentioning

confidence: 99%

Horizontal Basal Cell-Specific Deletion ofPax6Impedes Recovery of the Olfactory Neuroepithelium Following Severe Injury

Suzuki

Sakurai

Yamazaki

et al. 2015

Stem Cells and Development

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In the mammalian olfactory epithelium (OE), olfactory receptor neurons (ORNs) are continuously regenerated throughout the animal's lifetime. Horizontal basal cells (HBCs) in the OE express the epithelial marker keratin 5 (K5) and the stem cell marker Pax6 and are considered relatively quiescent tissue stem cells in the OE. Pax6 is a key regulator of several developmental processes in the central nervous system and in sensory organs. Although Pax6 is expressed in the OE, its precise role remains unknown, particularly with respect to stem celllike HBCs. To investigate the function of Pax6 in the developmental and regenerative processes in the OE, we generated conditional Pax6-knockout mice carrying a loxP-floxed Pax6 gene. Homozygous Pax6-floxed mice were crossed with K5-Cre transgenic mice to generate HBC-specific Pax6-knockout (Pax6-cKO) mice. We confirmed that the deletion of Pax6 expression in HBCs was sufficiently achieved in zone 1 of the OE in Pax6-cKO mice 3 days after methimazole-induced severe damage. In this condition, regeneration of the OE was dramatically impaired; both OE thickness and the number of ORNs were significantly decreased in the regenerated OE of Pax6-cKO mice. These results suggest that Pax6 expression is essential for HBCs to differentiate into neuronal cells during the regeneration process following severe injury.

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“…for the development of various tissues and organs, particularly the eye and the nervous system (18,20,(27)(28)(29)(30)(31). Here we reported a new splicing isoform of Pax6, Pax6(S), whose C terminus (PST N S) is composed of a truncated canonical PST domain and a unique S tail.…”

Section: Pax6(s) Is a Novel Splicing Isoform Of Pax6-pax6 Is Criticalmentioning

confidence: 99%

The β Subunit of Voltage-gated Ca2+ Channels Interacts with and Regulates the Activity of a Novel Isoform of Pax6

Zhang¹,

Yamada²,

Fan

et al. 2010

Journal of Biological Chemistry

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Ca2؉ channel ␤ subunits (Ca v ␤s) are essential for regulating the surface expression and gating of high voltage-activated Ca 2؉ channels through their interaction with Ca 2؉ channel ␣ 1 subunits. In efforts to uncover new interacting partners and new functions for Ca v ␤, we identified a new splicing isoform of Pax6, a transcription factor crucial for the development of the eye, nose, brain, and pancreas. Pax6 contains two DNA binding domains (paired domain and homeodomain), a glycine-rich linker connecting these two domains and a C-terminal proline-, serine-, and threonine-rich transactivation domain. The protein sequence and function of Pax6 are highly conserved from invertebrate to human. The newly isolated isoform, named Pax6(S), retains the paired domain, linker, and homeodomain of Pax6, but its C terminus is composed of a truncated classic proline, serine, and threonine domain and a unique S tail. Pax6(S) shows a similar level of transcriptional activity in vitro as does Pax6, but only in primates is the protein sequence highly conserved. Its spatial-temporal expression profiles are also different from those of Pax6. These divergences suggest a noncanonical role of Pax6(S) during development. The interaction between Pax6(S) and Ca v ␤ is mainly endowed by the S tail. Co-expression of Pax6(S) with a Ca 2؉ channel complex containing the ␤ 3 subunit in Xenopus oocytes does not affect channel properties. Conversely, however, ␤ 3 is able to suppress the transcriptional activity of Pax6(S). Furthermore, in the presence of Pax6(S), ␤ 3 is translocated from the cytoplasm to the nucleus. These results suggest that full-length Ca v ␤ may act directly as a transcription regulator independent of its role in regulating Ca 2؉ channel activity.4 is a cytosolic auxiliary protein of multimeric high voltage-activated (HVA) Ca 2ϩ channel complexes, which include L-, N-, P/Q-, and R-type Ca 2ϩ channels. It plays an essential role in chaperoning the channel complex to the plasma membrane and normalizing its gating properties (1-4). Crystal structures of Ca v ␤ in complex with its high affinity binding site in the principal poreforming ␣ 1 subunit (Ca v ␣ 1 ) show that much of the exposed surface of Ca v ␤ is unoccupied and is available to engage in interactions with other regions of Ca v ␣ 1 or with other proteins (5-7). Indeed, an increasing number of proteins has been shown to directly interact with Ca v ␤, including the Rem/Rad/Gem/Kir (RGK) family of small monomeric GTPases (8, 9), RIM1 (10), ryanodine receptors (11), Ahnak (12, 13), bestrophin-1 (14), and dynamin (15). Many of these proteins have been reported to regulate the activity of HVA Ca 2ϩ channels. To search for other potential Ca v ␤-interacting proteins, we carried out yeast two-hybrid screens using the ␤ 3 subunit as bait. Among the candidate target proteins we isolated, one was related to Pax6.Pax6 is a transcription factor that belongs to the paired box (Pax) family (16 -25). It is widely expressed in the eye, nose, pancreas, and the central nervous system ...

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Role of a transcription factor Pax6 in the developing vertebrate olfactory system

Cited by 48 publications

References 75 publications

The Orchestration of Mammalian Tissue Morphogenesis through a Series of Coherent Feed-forward Loops

The Orchestration of Mammalian Tissue Morphogenesis through a Series of Coherent Feed-forward Loops

Horizontal Basal Cell-Specific Deletion ofPax6Impedes Recovery of the Olfactory Neuroepithelium Following Severe Injury

The β Subunit of Voltage-gated Ca2+ Channels Interacts with and Regulates the Activity of a Novel Isoform of Pax6

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