Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase

Yaghootfam A, Schestag F, Dierks T, Gieselmann V (2003)
JOURNAL OF BIOLOGICAL CHEMISTRY 278(35): 32653-32661.

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Abstract
The critical step for sorting of lysosomal enzymes is the recognition by a Golgi-located phosphotransferase. The topogenic structure common to all lysosomal enzymes essential for this recognition is still not well defined, except that lysine residues seem to play a critical role. Here we have substituted surface-located lysine residues of lysosomal arylsulfatases A and B. In lysosomal arylsulfatase A only substitution of lysine residue 457 caused a reduction of phosphorylation to 33% and increased secretion of the mutant enzyme. In contrast to critical lysines in various other lysosomal enzymes, lysine 457 is not located in an unstructured loop region but in a helix. It is not strictly conserved among six homologous lysosomal sulfatases. Based on three-dimensional structure comparison, lysines 497 and 507 in arylsulfatase B are in a similar position as lysine 457 of arylsulfatase A. Also, the position of oligosaccharide side chains phosphorylated in arylsulfatase A is similar in arylsulfatase B. Despite the high degree of structural homology between these two sulfatases substitution of lysines 497 and 507 in arylsulfatase B has no effect on the sorting and phosphorylation of this sulfatase. Thus, highly homologous lysosomal arylsulfatases A and B did not develop a single conserved phosphotransferase recognition signal, demonstrating the high variability of this signal even in evolutionary closely related enzymes.
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Yaghootfam A, Schestag F, Dierks T, Gieselmann V. Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase. JOURNAL OF BIOLOGICAL CHEMISTRY. 2003;278(35):32653-32661.
Yaghootfam, A., Schestag, F., Dierks, T., & Gieselmann, V. (2003). Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase. JOURNAL OF BIOLOGICAL CHEMISTRY, 278(35), 32653-32661.
Yaghootfam, A., Schestag, F., Dierks, T., and Gieselmann, V. (2003). Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase. JOURNAL OF BIOLOGICAL CHEMISTRY 278, 32653-32661.
Yaghootfam, A., et al., 2003. Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase. JOURNAL OF BIOLOGICAL CHEMISTRY, 278(35), p 32653-32661.
A. Yaghootfam, et al., “Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 278, 2003, pp. 32653-32661.
Yaghootfam, A., Schestag, F., Dierks, T., Gieselmann, V.: Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase. JOURNAL OF BIOLOGICAL CHEMISTRY. 278, 32653-32661 (2003).
Yaghootfam, A, Schestag, F, Dierks, Thomas, and Gieselmann, V. “Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine : lysosomal enzyme N-acetylglucosamine-phosphotransferase”. JOURNAL OF BIOLOGICAL CHEMISTRY 278.35 (2003): 32653-32661.
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