CLN-encoded proteins do not interact with each other
| Autor: | Ju W, Moroziewicz Dn, Wisniewski Ke, Zhong Na, Jurkiewicz A, Brown Wt |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Two-hybrid screening
engineering.material Biology medicine.disease_cause Protein–protein interaction Cellular and Molecular Neuroscience Open Reading Frames Neuronal Ceroid-Lipofuscinoses Genetics medicine Humans Cloning Molecular Gene Genetics (clinical) Mutation Tripeptidyl-Peptidase 1 Reverse Transcriptase Polymerase Chain Reaction Chromosome Mapping Membrane Proteins medicine.disease Phenotype Batten CLN3 engineering Neuronal ceroid lipofuscinosis Lysosomes |
| Zdroj: | Neurogenetics. 3(1) |
| ISSN: | 1364-6745 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink