Gaucher disease: forging a new path to the lysosome - PubMed (original) (raw)
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. 2007 Nov 16;131(4):647-9.
doi: 10.1016/j.cell.2007.10.043.
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- PMID: 18022357
- DOI: 10.1016/j.cell.2007.10.043
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Gaucher disease: forging a new path to the lysosome
Gillian M Griffiths. Cell. 2007.
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Abstract
Most lysosomal proteins are tagged with a carbohydrate modification that allows their recognition and transport to the lysosome. In this issue, Reczek et al. (2007) identify a new pathway for protein sorting to the lysosome. They show that beta-glucocerebrosidase-the lysosomal enzyme defective in patients with Gaucher disease-is delivered to the lysosome through its interaction with the transmembrane protein LIMP-2.
Comment on
- LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase.
Reczek D, Schwake M, Schröder J, Hughes H, Blanz J, Jin X, Brondyk W, Van Patten S, Edmunds T, Saftig P. Reczek D, et al. Cell. 2007 Nov 16;131(4):770-83. doi: 10.1016/j.cell.2007.10.018. Cell. 2007. PMID: 18022370
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