ABSTRACT
The lysosomal storage of lipofuscins is the common pathological feature that characterizes the infantile, late-infantile, juvenile (Batten's disease), and Finnish-variant neuronal ceroid lipofuscinosis (INCL, LINCL, JNCL and FNCL), which are due to mutations in the genes CLN1 , CLN2 , CLN3 , and CLN5 , respectively. The CLN1 and CLN2 genes encode lysosomal enzymes, but the CLN3 and CLN5 genes encode membrane-spanning proteins. Why deficiencies of lysosomal enzymes and membrane-spanning proteins produce similar clinical phenotypes and pathological changes is still unanswered. We hypothesize that CLN -encoded proteins may comprise a functional pathogenic pathway, in which protein associations may play important roles. To test this hypothesis, we studied protein-protein interactions among the CLN1 -, CLN2 -, and CLN3 -encoded proteins using a yeast two-hybrid system. Our results provided no evidence that CLN -encoded proteins interact with each other. This suggests there may be unidentified components in NCL pathogenesis.
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Received: December 1, 1999 / Accepted: February 2, 2000 / Published online: May 9, 2000
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Zhong, N., Moroziewicz, D., Ju, W. et al. CLN -encoded proteins do not interact with each other. Neurogenetics 3, 41–44 (2000). https://doi.org/10.1007/PL00022978
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DOI: https://doi.org/10.1007/PL00022978