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Updated: Aug 8, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
Identification of a transactivation motif in the CLN3 protein
K Y Leung1, N D Greene, P B Munroe
1Department of Paediatrics, Royal Free and University College London Medical School, Rayne Institute, United Kingdom. kit-yi.leung@harefield.nthames.nhs.uk
Abstract:
A transactivation motif has been identified in the neurodegenerative disease protein, CLN3. The C-terminal domain (residues 394-438) of CLN3 can function as a transcriptional activator when fused to the DNA binding domain, LexA. A series of deletion and substitution constructs have been generated to identify the essential region for transactivation. A similar motif is also present in the POU domain transcription factor, nubbin. However, this domain alone does not activate transcription, allowing further localisation of the critical residues in CLN3 required for activity.
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