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.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Yaghootfam, A; Schestag, F; Dierks, ThomasUniBi; Gieselmann, V
Abstract / Bemerkung
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.
Erscheinungsjahr
2003
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
278
Ausgabe
35
Seite(n)
32653-32661
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/2350753

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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. https://doi.org/10.1074/jbc.M304865200
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.

6 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module.
Qian Y, Flanagan-Steet H, van Meel E, Steet R, Kornfeld SA., Proc Natl Acad Sci U S A 110(25), 2013
PMID: 23733939
High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting.
Hassan MI, Waheed A, Grubb JH, Klei HE, Korolev S, Sly WS., PLoS One 8(11), 2013
PMID: 24260279
Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase.
Qian Y, Lee I, Lee WS, Qian M, Kudo M, Canfield WM, Lobel P, Kornfeld S., J Biol Chem 285(5), 2010
PMID: 19955174
Sulfatide is required for efficient replication of influenza A virus.
Takahashi T, Murakami K, Nagakura M, Kishita H, Watanabe S, Honke K, Ogura K, Tai T, Kawasaki K, Miyamoto D, Hidari KI, Guo CT, Suzuki Y, Suzuki T., J Virol 82(12), 2008
PMID: 18417587
Identification of sites of mannose 6-phosphorylation on lysosomal proteins.
Sleat DE, Zheng H, Qian M, Lobel P., Mol Cell Proteomics 5(4), 2006
PMID: 16399764

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