Localization of active endogenous and exogenous β‐glucocerebrosidase by correlative light‐electron microscopy in human fibroblasts

Author:

van Meel Eline1ORCID,Bos Erik2,van der Lienden Martijn J. C.1,Overkleeft Herman S.3,van Kasteren Sander I.3,Koster Abraham J.2,Aerts Johannes M. F. G.1

Affiliation:

1. Department of Medical Biochemistry, Leiden Institute of ChemistryLeiden University Leiden the Netherlands

2. Department of Cell and Chemical BiologyLeiden University Medical Center Leiden the Netherlands

3. Department of Bio‐organic Synthesis, Leiden Institute of ChemistryLeiden University Leiden the Netherlands

Funder

H2020 European Research Council

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology

Reference30 articles.

1. Glucocerebrosidase, a lysosomal enzyme that does not undergo oligosaccharide phosphorylation

2. Mannose 6‐phosphate‐independent membrane association of cathepsin D, glucocerebrosidase, and sphingolipid‐activating protein in HepG2 cells;Rijnboutt S;J Biol Chem,1991

3. Mannose 6‐phosphate‐independent targeting of cathepsin D to lysosomes in HepG2 cells;Rijnboutt S;J Biol Chem,1991

4. LIMP-2 Is a Receptor for Lysosomal Mannose-6-Phosphate-Independent Targeting of β-Glucocerebrosidase

5. Lysosomal targeting of Limp II membrane glycoprotein requires a novel Leu‐Ile motif at a particular position in its cytoplasmic tail;Ogata S;J Biol Chem,1994

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