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Title: Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease.
Austin Authors: Peters, Judith;Rittger, Andrea;Weisner, Rebecca;Knabbe, Johannes;Zunke, Friederike;Rothaug, Michelle;Damme, Markus;Berkovic, Samuel F ;Blanz, Judith;Saftig, Paul;Schwake, Michael
Affiliation: Epilepsy Research Centre, Department of Medicine, University of Melbourne, Austin Health, Heidelberg 3084, Australia
Institut für Biochemie, Christian-Albrechts-Universität zu Kiel, Olshausenstrasse 40, D-24098 Kiel, Germany.
Biochemie III, Fakultät für Chemie, Universität Bielefeld, Universitätsstr. 25, D-33615, Germany
Issue Date: 7-Jan-2015
Publication information: Biochemical and Biophysical Research Communications 2015; 457(3): 334-40
Abstract: The lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) has been identified as a receptor for enterovirus 71 uptake and mannose-6-phosphate-independent lysosomal trafficking of the acid hydrolase β-glucocerebrosidase. Here we show that LIMP-2 undergoes proteolytic cleavage mediated by lysosomal cysteine proteases. Heterologous expression and in vitro studies suggest that cathepsin-F is mainly responsible for the lysosomal processing of wild-type LIMP-2. Furthermore, examination of purified lysosomes revealed that LIMP-2 undergoes proteolysis in vivo. Mutations in the gene encoding cathepsin-F (CTSF) have recently been associated with type-B-Kufs-disease, an adult form of neuronal ceroid-lipofuscinosis. In this study we show that disease-causing cathepsin-F mutants fail to cleave LIMP-2. Our findings provide evidence that LIMP-2 represents an in vivo substrate of cathepsin-F with relevance for understanding the pathophysiology of type-B-Kufs-disease.
Gov't Doc #: 25576872
DOI: 10.1016/j.bbrc.2014.12.111
Type: Journal Article
Subjects: Cathepsin-F
Kufs disease
Lysosomal storage disease
Neuronal ceroid-lipofuscinosis
Appears in Collections:Journal articles

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