Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY

Kowalewski B, Lübke T, Kollmann K, Braulke T, Reinheckel T, Dierks T, Damme M (2014)
The Journal of biological chemistry 289(40): 27992-28005.

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Arylsulfatase G (ARSG) is a recently identified lysosomal sulfatase that was shown to be responsible for the degradation of 3-O-sulfated N-sulfoglucosamine residues of heparan sulfate glycosaminoglycans. Deficiency of ARSG leads to a new type of mucopolysaccharidosis, as described in a mouse model. Here, we provide a detailed molecular characterization of the endogenous murine enzyme. ARSG is expressed and proteolytically processed in a tissue-specific manner. The 63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes, most likely the endoplasmic reticulum. In contrast, proteolytically processed ARSG fragments of 34-, 18-, and 10-kDa were found in lysosomal fractions and lost their membrane association. The processing sites and a disulfide bridge between the 18- and 10-kDa chains could be roughly mapped. Proteases participating in the processing were identified as cathepsins B and L. Proteolytic processing is dispensable for hydrolytic sulfatase activity in vitro. Lysosomal transport of ARSG in the liver is independent of mannose 6-phosphate, sortilin, and Limp2. However, mutation of glycosylation site N-497 abrogates transport of ARSG to lysosomes in human fibrosarcoma cells, due to impaired mannose 6-phosphate modification.
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Kowalewski B, Lübke T, Kollmann K, et al. Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry. 2014;289(40):27992-28005.
Kowalewski, B., Lübke, T., Kollmann, K., Braulke, T., Reinheckel, T., Dierks, T., & Damme, M. (2014). Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry, 289(40), 27992-28005. doi:10.1074/jbc.M114.584144
Kowalewski, B., Lübke, T., Kollmann, K., Braulke, T., Reinheckel, T., Dierks, T., and Damme, M. (2014). Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry 289, 27992-28005.
Kowalewski, B., et al., 2014. Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry, 289(40), p 27992-28005.
B. Kowalewski, et al., “Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY”, The Journal of biological chemistry, vol. 289, 2014, pp. 27992-28005.
Kowalewski, B., Lübke, T., Kollmann, K., Braulke, T., Reinheckel, T., Dierks, T., Damme, M.: Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry. 289, 27992-28005 (2014).
Kowalewski, Björn, Lübke, Torben, Kollmann, Katrin, Braulke, Thomas, Reinheckel, Thomas, Dierks, Thomas, and Damme, Markus. “Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY”. The Journal of biological chemistry 289.40 (2014): 27992-28005.
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