CLN-encoded proteins do not interact with each other.
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.
Zhong
N A
NA
Molecular Neurogenetic Diagnostic Laboratory, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, USA. omrddzhong@aol.com
Moroziewicz
D N
DN
Ju
W
W
Wisniewski
K E
KE
Jurkiewicz
A
A
Brown
W T
WT
D002874:Chromosome Mapping; D003001:Cloning, Molecular; D006801:Humans; D008247:Lysosomes / Q000201:enzymology; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D009472:Neuronal Ceroid-Lipofuscinoses / Q000235:genetics*; D016366:Open Reading Frames; D020133:Reverse Transcriptase Polymerase Chain Reaction; D000091346:Tripeptidyl-Peptidase 1
D008565:Membrane Proteins; D000091346:Tripeptidyl-Peptidase 1; C000717267:TPP1 protein, human