Abstract
Neuronal ceroid lipofuscinoses (NCL) are caused by mutations in eight different genes, are characterized by lysosomal accumulation of autofluorescent storage material, and result in a disease that causes degeneration of the central nervous system (CNS). Although functions are defined for some of the soluble proteins that are defective in NCL (cathepsin D, PPT1, and TPP1), the primary function of the other proteins defective in NCLs (CLN3, CLN5, CLN6, CLN7, and CLN8) remain poorly defined. Understanding the localization and network of interactions for these proteins can offer clues as to the function of the NCL proteins and also the pathways that will be disrupted in their absence. Here, we present a review of the current understanding of the localization, interactions, and function of the proteins associated with NCL.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Aminopeptidases / analysis
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Aminopeptidases / genetics
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Aminopeptidases / metabolism*
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Animals
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Cathepsin D / analysis
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Cathepsin D / genetics
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Cathepsin D / metabolism*
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / analysis
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / genetics
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism*
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Humans
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Lysosomes / genetics
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Lysosomes / metabolism
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Lysosomes / pathology
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Membrane Proteins / analysis
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Neuronal Ceroid-Lipofuscinoses / genetics
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Neuronal Ceroid-Lipofuscinoses / metabolism*
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Protein Interaction Mapping
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Serine Proteases / analysis
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Serine Proteases / genetics
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Serine Proteases / metabolism*
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Thiolester Hydrolases / analysis
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Thiolester Hydrolases / genetics
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Thiolester Hydrolases / metabolism*
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Tripeptidyl-Peptidase 1
Substances
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Membrane Proteins
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Tripeptidyl-Peptidase 1
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Thiolester Hydrolases
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palmitoyl-protein thioesterase
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Serine Proteases
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Aminopeptidases
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
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TPP1 protein, human
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Cathepsin D