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Biochim Biophys Acta. 2015 Oct;1852(10 Pt B):2242-55. doi: 10.1016/j.bbadis.2015.04.027. Epub 2015 May 8.

Cell biology of the NCL proteins: What they do and don't do.

Author information

1
Sanford Children's Health Research Center, Sanford Research, Sioux Falls, SD, 57104, USA.
2
Sanford Children's Health Research Center, Sanford Research, Sioux Falls, SD, 57104, USA; Department of Pediatrics, Sanford School of Medicine, University of South Dakota, Sioux Falls, SD, 57104, USA. Electronic address: David.Pearce@sanfordhealth.org.

Abstract

The fatal, primarily childhood neurodegenerative disorders, neuronal ceroid lipofuscinoses (NCLs), are currently associated with mutations in 13 genes. The protein products of these genes (CLN1 to CLN14) differ in their function and their intracellular localization. NCL-associated proteins have been localized mostly in lysosomes (CLN1, CLN2, CLN3, CLN5, CLN7, CLN10, CLN12 and CLN13) but also in the Endoplasmic Reticulum (CLN6 and CLN8), or in the cytosol associated to vesicular membranes (CLN4 and CLN14). Some of them such as CLN1 (palmitoyl protein thioesterase 1), CLN2 (tripeptidyl-peptidase 1), CLN5, CLN10 (cathepsin D), and CLN13 (cathepsin F), are lysosomal soluble proteins; others like CLN3, CLN7, and CLN12, have been proposed to be lysosomal transmembrane proteins. In this review, we give our views and attempt to summarize the proposed and confirmed functions of each NCL protein and describe and discuss research results published since the last review on NCL proteins. This article is part of a Special Issue entitled: "Current Research on the Neuronal Ceroid Lipofuscinoses (Batten Disease)".

KEYWORDS:

Batten disease; CLN1-14; NCL proteins; Neuronal ceroid lipofuscinoses

PMID:
25962910
DOI:
10.1016/j.bbadis.2015.04.027
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