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two-hybrid screening\nWe hypothesised that the C-terminal peptide might be involved in protein-protein interactions, and we tested this by screening a cDNA library using the yeast two-hybrid system with a construct (PAX6CTP) in which the 32 amino acid C-terminal peptide was fused to the yeast GAL4 DNA binding domain. We chose to screen a mouse brain cDNA library as no human libraries were available. Given the fact that the amino acid sequence of the PAX6 protein is identical in man and mouse, we reasoned that a mouse brain library would yield relevant interactors. For comparison we also carried out the screen using a construct containing the whole PST domain (PAX6PST).\nThe C-terminal peptide screen gave 15 colonies that were positive with all three reporters and the PST domain screen gave 62 colonies. The interacting plasmids were isolated and the cDNA inserts sequenced. Three cDNAs were identified 3 or more times, Homer3 (NM_011984), Dncl1 (Dynein cytoplasmic light chain 1, NM_019682, also known as Pin or Dlc8) and Trim11 (Tripartite motif protein family member 11, NM_053168). Homer3 (6 clones) and Dncl1 (2 clones) were identified in the C-terminal peptide screen. Homer3 (7 clones), Dncl1 (2 clones) and Trim11 (6 clones) were identified in the PST domain screen. All cDNA inserts were in-frame with the coding region of the pPC86 GAL4 activation domain. None of the cDNAs was present in a list of known false positives [34].\nHOMER3 is a member of the HOMER family of neuronal post-synaptic density (PSD) proteins [35]. DNCL1 is a subunit of two motor protein complexes, dynein and myosin-Va, both of which are involved in intracellular trafficking of proteins and organelles in neurons [36,37]. TRIM11 is a member of the tripartite motif protein family and contains a RING finger, a B-box zinc finger, a coiled coil domain and a B30.2 domain [38]. The possible significance of the interactions between these proteins and PAX6 is discussed below."}

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All cDNA inserts were in-frame with the coding region of the pPC86 GAL4 activation domain. None of the cDNAs was present in a list of known false positives [34].\nHOMER3 is a member of the HOMER family of neuronal post-synaptic density (PSD) proteins [35]. DNCL1 is a subunit of two motor protein complexes, dynein and myosin-Va, both of which are involved in intracellular trafficking of proteins and organelles in neurons [36,37]. TRIM11 is a member of the tripartite motif protein family and contains a RING finger, a B-box zinc finger, a coiled coil domain and a B30.2 domain [38]. The possible significance of the interactions between these proteins and PAX6 is discussed below."}

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We chose to screen a mouse brain cDNA library as no human libraries were available. Given the fact that the amino acid sequence of the PAX6 protein is identical in man and mouse, we reasoned that a mouse brain library would yield relevant interactors. For comparison we also carried out the screen using a construct containing the whole PST domain (PAX6PST).\nThe C-terminal peptide screen gave 15 colonies that were positive with all three reporters and the PST domain screen gave 62 colonies. The interacting plasmids were isolated and the cDNA inserts sequenced. Three cDNAs were identified 3 or more times, Homer3 (NM_011984), Dncl1 (Dynein cytoplasmic light chain 1, NM_019682, also known as Pin or Dlc8) and Trim11 (Tripartite motif protein family member 11, NM_053168). Homer3 (6 clones) and Dncl1 (2 clones) were identified in the C-terminal peptide screen. Homer3 (7 clones), Dncl1 (2 clones) and Trim11 (6 clones) were identified in the PST domain screen. 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