Publication

Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex

Sprong, H., Degroote, S., Claessens, T., Oorschot, V., Westerink, B. H. C., Hirabayashi, Y., Klumperman, J., van der Sluijs, P. & van Meer, G., 29-Oct-2001, In : Journal of Cell Biology. 155, 3, p. 369-379 11 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Sprong, H., Degroote, S., Claessens, T., Oorschot, V., Westerink, B. H. C., Hirabayashi, Y., Klumperman, J., van der Sluijs, P., & van Meer, G. (2001). Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex. Journal of Cell Biology, 155(3), 369-379. https://doi.org/10.1083/jcb.200106104

Author

Sprong, H. ; Degroote, S. ; Claessens, T. ; Oorschot, V. ; Westerink, B. H. C. ; Hirabayashi, Y. ; Klumperman, J. ; van der Sluijs, P. ; van Meer, G. / Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex. In: Journal of Cell Biology. 2001 ; Vol. 155, No. 3. pp. 369-379.

Harvard

Sprong, H, Degroote, S, Claessens, T, Oorschot, V, Westerink, BHC, Hirabayashi, Y, Klumperman, J, van der Sluijs, P & van Meer, G 2001, 'Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex', Journal of Cell Biology, vol. 155, no. 3, pp. 369-379. https://doi.org/10.1083/jcb.200106104

Standard

Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex. / Sprong, H.; Degroote, S.; Claessens, T.; Oorschot, V.; Westerink, B. H. C.; Hirabayashi, Y.; Klumperman, J.; van der Sluijs, P.; van Meer, G.

In: Journal of Cell Biology, Vol. 155, No. 3, 29.10.2001, p. 369-379.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Sprong H, Degroote S, Claessens T, Oorschot V, Westerink BHC, Hirabayashi Y et al. Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex. Journal of Cell Biology. 2001 Oct 29;155(3):369-379. https://doi.org/10.1083/jcb.200106104


BibTeX

@article{49fa3f65e0794fd18e99ca8221161bc8,
title = "Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex",
abstract = "Although glycosphingolipids are ubiquitously expressed and essential for multicellular organisms, surprisingly little is known about their intracellular functions. To explore the role of glycosphingolipids in membrane transport, we used the glycosphingolipid-deficient GM95 mouse melanoma cell line. We found that GM95 cells do not make melanin pigment because tyrosinase, the first and rate-limiting enzyme in melanin synthesis, was not targeted to melanosomes but accumulated in the Golgi complex. However, tyrosinase-related protein 1 still reached melanosomal structures via the plasma membrane instead of the direct pathway from the Golgi. Delivery of lysosomal enzymes from the Golgi complex to endosomes was normal, suggesting that this pathway is not affected by the absence of glycosphingolipids. Loss of pigmentation was due to tyrosinase mislocalization, since transfection of tyrosinase with an extended transmembrane domain, which bypassed the transport block, restored pigmentation. Transfection of ceramide glucosyltransferase or addition of glucosylsphingosine restored tyrosinase transport and pigmentation. We conclude that protein transport from Golgi to melanosomes via the direct pathway requires glycosphingolipids.",
keywords = "glycosphingolipid, protein sorting, melanosome, tyrosinase, TRP-1, TYROSINASE-RELATED PROTEIN-1, MOUSE MELANOMA-CELLS, DI-LEUCINE, MDCK CELLS, CERAMIDE GALACTOSYLTRANSFERASE, CYTOPLASMIC TAIL, EPITHELIAL-CELLS, MEMBRANE RAFTS, AP-3 ADAPTER, TRANSPORT",
author = "H. Sprong and S. Degroote and T. Claessens and V. Oorschot and Westerink, {B. H. C.} and Y. Hirabayashi and J. Klumperman and {van der Sluijs}, P. and {van Meer}, G.",
year = "2001",
month = oct,
day = "29",
doi = "10.1083/jcb.200106104",
language = "English",
volume = "155",
pages = "369--379",
journal = "The Journal of Cell Biology",
issn = "0021-9525",
publisher = "ROCKEFELLER UNIV PRESS",
number = "3",

}

RIS

TY - JOUR

T1 - Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex

AU - Sprong, H.

AU - Degroote, S.

AU - Claessens, T.

AU - Oorschot, V.

AU - Westerink, B. H. C.

AU - Hirabayashi, Y.

AU - Klumperman, J.

AU - van der Sluijs, P.

AU - van Meer, G.

PY - 2001/10/29

Y1 - 2001/10/29

N2 - Although glycosphingolipids are ubiquitously expressed and essential for multicellular organisms, surprisingly little is known about their intracellular functions. To explore the role of glycosphingolipids in membrane transport, we used the glycosphingolipid-deficient GM95 mouse melanoma cell line. We found that GM95 cells do not make melanin pigment because tyrosinase, the first and rate-limiting enzyme in melanin synthesis, was not targeted to melanosomes but accumulated in the Golgi complex. However, tyrosinase-related protein 1 still reached melanosomal structures via the plasma membrane instead of the direct pathway from the Golgi. Delivery of lysosomal enzymes from the Golgi complex to endosomes was normal, suggesting that this pathway is not affected by the absence of glycosphingolipids. Loss of pigmentation was due to tyrosinase mislocalization, since transfection of tyrosinase with an extended transmembrane domain, which bypassed the transport block, restored pigmentation. Transfection of ceramide glucosyltransferase or addition of glucosylsphingosine restored tyrosinase transport and pigmentation. We conclude that protein transport from Golgi to melanosomes via the direct pathway requires glycosphingolipids.

AB - Although glycosphingolipids are ubiquitously expressed and essential for multicellular organisms, surprisingly little is known about their intracellular functions. To explore the role of glycosphingolipids in membrane transport, we used the glycosphingolipid-deficient GM95 mouse melanoma cell line. We found that GM95 cells do not make melanin pigment because tyrosinase, the first and rate-limiting enzyme in melanin synthesis, was not targeted to melanosomes but accumulated in the Golgi complex. However, tyrosinase-related protein 1 still reached melanosomal structures via the plasma membrane instead of the direct pathway from the Golgi. Delivery of lysosomal enzymes from the Golgi complex to endosomes was normal, suggesting that this pathway is not affected by the absence of glycosphingolipids. Loss of pigmentation was due to tyrosinase mislocalization, since transfection of tyrosinase with an extended transmembrane domain, which bypassed the transport block, restored pigmentation. Transfection of ceramide glucosyltransferase or addition of glucosylsphingosine restored tyrosinase transport and pigmentation. We conclude that protein transport from Golgi to melanosomes via the direct pathway requires glycosphingolipids.

KW - glycosphingolipid

KW - protein sorting

KW - melanosome

KW - tyrosinase

KW - TRP-1

KW - TYROSINASE-RELATED PROTEIN-1

KW - MOUSE MELANOMA-CELLS

KW - DI-LEUCINE

KW - MDCK CELLS

KW - CERAMIDE GALACTOSYLTRANSFERASE

KW - CYTOPLASMIC TAIL

KW - EPITHELIAL-CELLS

KW - MEMBRANE RAFTS

KW - AP-3 ADAPTER

KW - TRANSPORT

U2 - 10.1083/jcb.200106104

DO - 10.1083/jcb.200106104

M3 - Article

VL - 155

SP - 369

EP - 379

JO - The Journal of Cell Biology

JF - The Journal of Cell Biology

SN - 0021-9525

IS - 3

ER -

ID: 3975757