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PAX6 protein is a member of the PAX (paired-box) family of transcriptional regulators and is essential for normal ocular and neural development [1]. Heterozygous mutations of the human PAX6 gene cause aniridia (absence of the iris) and a range of other congenital eye malformations [2]. Neural defects such as foveal hypoplasia and optic nerve hypoplasia are common in PAX6-associated eye disease [3-5]. Homozygous mutations in man and mouse are lethal and result in severe developmental abnormalities including anophthalmia, severe reduction of the olfactory structures and gross brain malformations [2,6]. The roles of PAX6 in brain development have mainly been studied in homozygous mutant mice or rats and include arealisation of the cerebral cortex [7], formation of the prosencephalon-mesencephalon boundary [8], axon guidance [8], differentiation of neurons from glia [9] and neuronal migration in the cerebellum [10].\nThe discovery of multiple and diverse roles for PAX6 in brain development prompted MRI analyses of aniridia patients, and a range of distinctive brain anomalies were uncovered. The most common and striking of these was absence or hypoplasia of the anterior commissure [11]. Other defects included absence or hypoplasia of the pineal gland, cortical polymicrogyria, white matter changes in the corpus callosum and grey matter changes in the cerebellum [11-13]. Functional changes included hyposmia and abnormal inter-hemispheric auditory transfer [11,14].\nThe defining feature of all PAX proteins is the presence of a 128 amino acid DNA-binding paired domain that has been highly conserved over evolution [1]. In addition to the paired domain, PAX6 also contains a DNA-binding homeodomain and a proline, serine and threonine-rich (PST) domain at the C-terminus [1,6]. The PST domain, which encompasses the C-terminal 145 amino acids of PAX6, has been shown to act as a transcriptional activator [6]. The PAX6 protein directly regulates a wide range of target genes [1,2] including Pax2 [15], Ngn2 [16] and glucagon [17].\nThe Pax6 gene has a spatially and temporally complex expression pattern in the eye, brain, nasal structures, spinal cord and pancreas [1]. Although PAX6 is clearly involved in multiple developmental processes, common themes are now emerging concerning the role of PAX6 in neural tissues. Gradients of Pax6 expression are important for determining positional characteristics in the retina [18] and the neocortex [7]. PAX6 plays a role in development of specific axonal connections between the retina and the brain [18] and within the forebrain [8,19]. It is also involved in the differentiation of neural cell types from multipotent precursors in the retina [16] and the cerebral cortex [9] through activation of bHLH genes such as Ngn2 and Mash1. These studies provide a clear link between PAX6 function in the retina and the brain, and are of particular relevance to the neurological phenotypes of individuals with PAX6 mutations.\nIt is becoming apparent that transcription factors do not act in isolation but are dependent on interactions with other proteins to carry out their function [20,21]. These interactions introduce more specificity into the regulatory function of a given transcription factor. To date only three PAX6 protein-protein interactions have been described: with SOX2 on the lens-specific enhancer element of the δ-crystallin gene [22]; with MDIA, which modulates PAX6 activity in early neuronal development [23], and with MAF proteins on the glucagon promoter, which causes increased expression of this pancreatic hormone gene [17].\nHere we report the preliminary results of the first systematic screen for proteins that interact with PAX6. We used sequence alignment algorithms and secondary structure prediction programs to define a new domain of 32 amino acids at the C-terminal end of the PAX6 protein. We then screened a brain library with this peptide using the yeast two-hybrid technique and identified three novel interacting proteins, HOMER3, DNCL1 and TRIM11. The interaction between PAX6 and these proteins was disrupted by naturally occurring C-terminal PAX6 mutations."}

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PAX6 protein is a member of the PAX (paired-box) family of transcriptional regulators and is essential for normal ocular and neural development [1]. Heterozygous mutations of the human PAX6 gene cause aniridia (absence of the iris) and a range of other congenital eye malformations [2]. Neural defects such as foveal hypoplasia and optic nerve hypoplasia are common in PAX6-associated eye disease [3-5]. Homozygous mutations in man and mouse are lethal and result in severe developmental abnormalities including anophthalmia, severe reduction of the olfactory structures and gross brain malformations [2,6]. The roles of PAX6 in brain development have mainly been studied in homozygous mutant mice or rats and include arealisation of the cerebral cortex [7], formation of the prosencephalon-mesencephalon boundary [8], axon guidance [8], differentiation of neurons from glia [9] and neuronal migration in the cerebellum [10].\nThe discovery of multiple and diverse roles for PAX6 in brain development prompted MRI analyses of aniridia patients, and a range of distinctive brain anomalies were uncovered. The most common and striking of these was absence or hypoplasia of the anterior commissure [11]. Other defects included absence or hypoplasia of the pineal gland, cortical polymicrogyria, white matter changes in the corpus callosum and grey matter changes in the cerebellum [11-13]. Functional changes included hyposmia and abnormal inter-hemispheric auditory transfer [11,14].\nThe defining feature of all PAX proteins is the presence of a 128 amino acid DNA-binding paired domain that has been highly conserved over evolution [1]. In addition to the paired domain, PAX6 also contains a DNA-binding homeodomain and a proline, serine and threonine-rich (PST) domain at the C-terminus [1,6]. The PST domain, which encompasses the C-terminal 145 amino acids of PAX6, has been shown to act as a transcriptional activator [6]. The PAX6 protein directly regulates a wide range of target genes [1,2] including Pax2 [15], Ngn2 [16] and glucagon [17].\nThe Pax6 gene has a spatially and temporally complex expression pattern in the eye, brain, nasal structures, spinal cord and pancreas [1]. Although PAX6 is clearly involved in multiple developmental processes, common themes are now emerging concerning the role of PAX6 in neural tissues. Gradients of Pax6 expression are important for determining positional characteristics in the retina [18] and the neocortex [7]. PAX6 plays a role in development of specific axonal connections between the retina and the brain [18] and within the forebrain [8,19]. It is also involved in the differentiation of neural cell types from multipotent precursors in the retina [16] and the cerebral cortex [9] through activation of bHLH genes such as Ngn2 and Mash1. These studies provide a clear link between PAX6 function in the retina and the brain, and are of particular relevance to the neurological phenotypes of individuals with PAX6 mutations.\nIt is becoming apparent that transcription factors do not act in isolation but are dependent on interactions with other proteins to carry out their function [20,21]. These interactions introduce more specificity into the regulatory function of a given transcription factor. To date only three PAX6 protein-protein interactions have been described: with SOX2 on the lens-specific enhancer element of the δ-crystallin gene [22]; with MDIA, which modulates PAX6 activity in early neuronal development [23], and with MAF proteins on the glucagon promoter, which causes increased expression of this pancreatic hormone gene [17].\nHere we report the preliminary results of the first systematic screen for proteins that interact with PAX6. We used sequence alignment algorithms and secondary structure prediction programs to define a new domain of 32 amino acids at the C-terminal end of the PAX6 protein. We then screened a brain library with this peptide using the yeast two-hybrid technique and identified three novel interacting proteins, HOMER3, DNCL1 and TRIM11. The interaction between PAX6 and these proteins was disrupted by naturally occurring C-terminal PAX6 mutations."}

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PAX6 protein is a member of the PAX (paired-box) family of transcriptional regulators and is essential for normal ocular and neural development [1]. Heterozygous mutations of the human PAX6 gene cause aniridia (absence of the iris) and a range of other congenital eye malformations [2]. Neural defects such as foveal hypoplasia and optic nerve hypoplasia are common in PAX6-associated eye disease [3-5]. Homozygous mutations in man and mouse are lethal and result in severe developmental abnormalities including anophthalmia, severe reduction of the olfactory structures and gross brain malformations [2,6]. The roles of PAX6 in brain development have mainly been studied in homozygous mutant mice or rats and include arealisation of the cerebral cortex [7], formation of the prosencephalon-mesencephalon boundary [8], axon guidance [8], differentiation of neurons from glia [9] and neuronal migration in the cerebellum [10].\nThe discovery of multiple and diverse roles for PAX6 in brain development prompted MRI analyses of aniridia patients, and a range of distinctive brain anomalies were uncovered. The most common and striking of these was absence or hypoplasia of the anterior commissure [11]. Other defects included absence or hypoplasia of the pineal gland, cortical polymicrogyria, white matter changes in the corpus callosum and grey matter changes in the cerebellum [11-13]. Functional changes included hyposmia and abnormal inter-hemispheric auditory transfer [11,14].\nThe defining feature of all PAX proteins is the presence of a 128 amino acid DNA-binding paired domain that has been highly conserved over evolution [1]. In addition to the paired domain, PAX6 also contains a DNA-binding homeodomain and a proline, serine and threonine-rich (PST) domain at the C-terminus [1,6]. The PST domain, which encompasses the C-terminal 145 amino acids of PAX6, has been shown to act as a transcriptional activator [6]. The PAX6 protein directly regulates a wide range of target genes [1,2] including Pax2 [15], Ngn2 [16] and glucagon [17].\nThe Pax6 gene has a spatially and temporally complex expression pattern in the eye, brain, nasal structures, spinal cord and pancreas [1]. Although PAX6 is clearly involved in multiple developmental processes, common themes are now emerging concerning the role of PAX6 in neural tissues. Gradients of Pax6 expression are important for determining positional characteristics in the retina [18] and the neocortex [7]. PAX6 plays a role in development of specific axonal connections between the retina and the brain [18] and within the forebrain [8,19]. It is also involved in the differentiation of neural cell types from multipotent precursors in the retina [16] and the cerebral cortex [9] through activation of bHLH genes such as Ngn2 and Mash1. These studies provide a clear link between PAX6 function in the retina and the brain, and are of particular relevance to the neurological phenotypes of individuals with PAX6 mutations.\nIt is becoming apparent that transcription factors do not act in isolation but are dependent on interactions with other proteins to carry out their function [20,21]. These interactions introduce more specificity into the regulatory function of a given transcription factor. To date only three PAX6 protein-protein interactions have been described: with SOX2 on the lens-specific enhancer element of the δ-crystallin gene [22]; with MDIA, which modulates PAX6 activity in early neuronal development [23], and with MAF proteins on the glucagon promoter, which causes increased expression of this pancreatic hormone gene [17].\nHere we report the preliminary results of the first systematic screen for proteins that interact with PAX6. We used sequence alignment algorithms and secondary structure prediction programs to define a new domain of 32 amino acids at the C-terminal end of the PAX6 protein. We then screened a brain library with this peptide using the yeast two-hybrid technique and identified three novel interacting proteins, HOMER3, DNCL1 and TRIM11. The interaction between PAX6 and these proteins was disrupted by naturally occurring C-terminal PAX6 mutations."}