Differential effects of lobe A and lobe B of the conserved oligomeric golgi complex on the stability of β1,4-galactosyltransferase 1 and α2,6-sialyltransferase 1

Peanne, Romain; Legrand, Dominique; Duvet, Sandrine; Mir, Anne-Marie; Matthijs, Gert; Rohrer, Jack; Foulquier, Francois

doi:10.21256/zhaw-3989

Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-3989

Publication type:	Article in scientific journal
Type of review:	Peer review (publication)
Title:	Differential effects of lobe A and lobe B of the conserved oligomeric golgi complex on the stability of β1,4-galactosyltransferase 1 and α2,6-sialyltransferase 1
Authors:	Peanne, Romain Legrand, Dominique Duvet, Sandrine Mir, Anne-Marie Matthijs, Gert Rohrer, Jack Foulquier, Francois
DOI:	10.21256/zhaw-3989 10.1093/glycob/cwq176
Published in:	Glycobiology
Volume(Issue):	21
Issue:	7
Page(s):	864
Pages to:	876
Issue Date:	8-Nov-2011
Publisher / Ed. Institution:	Oxford University Press
ISSN:	0959-6658 1460-2423
Language:	English
Subject (DDC):	572: Biochemistry
Abstract:	Initially described by Jaeken et al. in 1980, congenital disorders of glycosylation (CDG) is a rapidly expanding group of human multisystemic disorders. To date, many CDG patients have been identified with deficiencies in the conserved oligomeric Golgi (COG) complex which is a complex involved in the vesicular intra-Golgi retrograde trafficking. Composed of eight subunits that are organized in two lobes, COG subunit deficiencies have been associated with Golgi glycosylation abnormalities. Analysis of the total serum N-glycans of COG-deficient CDG patients demonstrated an overall decrease in terminal sialylation and galactosylation. According to the mutated COG subunits, differences in late Golgi glycosylation were observed and led us to address the question of an independent role and requirement for each of the two lobes of the COG complex in the stability and localization of late terminal Golgi glycosylation enzymes. For this, we used a small-interfering RNAs strategy in HeLa cells stably expressing green fluorescent protein (GFP)-tagged β1,4-galactosyltransferase 1 (B4GALT1) and α2,6-sialyltransferase 1 (ST6GAL1), two major Golgi glycosyltransferases involved in late Golgi N-glycosylation. Using fluorescent lectins and flow cytometry analysis, we clearly demonstrated that depletion of both lobes was associated with deficiencies in terminal Golgi N-glycosylation. Lobe A depletion resulted in dramatic changes in the Golgi structure, whereas lobe B depletion severely altered the stability of B4GALT1 and ST6GAL1. Only MG132 was able to rescue their steady-state levels, suggesting that B4GALT1- and ST6GAL1-induced degradation are likely the consequence of an accumulation in the endoplasmic reticulum (ER), followed by a retrotranslocation into the cytosol and proteasomal degradation. All together, our results suggest differential effects of lobe A and lobe B for the localization/stability of B4GALT1 and ST6GAL1. Lobe B would be crucial in preventing these two Golgi glycosyltransferases from inappropriate retrograde trafficking to the ER, whereas lobe A appears to be essential for maintaining the overall Golgi structure.
Further description:	Erworben im Rahmen der Schweizer Nationallizenzen (http://www.nationallizenzen.ch)
URI:	https://digitalcollection.zhaw.ch/handle/11475/6816
Fulltext version:	Published version
License (according to publishing contract):	Licence according to publishing contract
Departement:	Life Sciences and Facility Management
Organisational Unit:	Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:	Publikationen Life Sciences und Facility Management

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Peanne, R., Legrand, D., Duvet, S., Mir, A.-M., Matthijs, G., Rohrer, J., & Foulquier, F. (2011). Differential effects of lobe A and lobe B of the conserved oligomeric golgi complex on the stability of β1,4-galactosyltransferase 1 and α2,6-sialyltransferase 1. Glycobiology, 21(7), 864–876. https://doi.org/10.21256/zhaw-3989

Peanne, R. et al. (2011) ‘Differential effects of lobe A and lobe B of the conserved oligomeric golgi complex on the stability of β1,4-galactosyltransferase 1 and α2,6-sialyltransferase 1’, Glycobiology, 21(7), pp. 864–876. Available at: https://doi.org/10.21256/zhaw-3989.

R. Peanne et al., “Differential effects of lobe A and lobe B of the conserved oligomeric golgi complex on the stability of β1,4-galactosyltransferase 1 and α2,6-sialyltransferase 1,” Glycobiology, vol. 21, no. 7, pp. 864–876, Nov. 2011, doi: 10.21256/zhaw-3989.

PEANNE, Romain, Dominique LEGRAND, Sandrine DUVET, Anne-Marie MIR, Gert MATTHIJS, Jack ROHRER und Francois FOULQUIER, 2011. Differential effects of lobe A and lobe B of the conserved oligomeric golgi complex on the stability of β1,4-galactosyltransferase 1 and α2,6-sialyltransferase 1. Glycobiology. 8 November 2011. Bd. 21, Nr. 7, S. 864–876. DOI 10.21256/zhaw-3989

Peanne, Romain, Dominique Legrand, Sandrine Duvet, Anne-Marie Mir, Gert Matthijs, Jack Rohrer, and Francois Foulquier. 2011. “Differential Effects of Lobe A and Lobe B of the Conserved Oligomeric Golgi Complex on the Stability of Β1,4-Galactosyltransferase 1 and Α2,6-Sialyltransferase 1.” Glycobiology 21 (7): 864–76. https://doi.org/10.21256/zhaw-3989.

Peanne, Romain, et al. “Differential Effects of Lobe A and Lobe B of the Conserved Oligomeric Golgi Complex on the Stability of Β1,4-Galactosyltransferase 1 and Α2,6-Sialyltransferase 1.” Glycobiology, vol. 21, no. 7, Nov. 2011, pp. 864–76, https://doi.org/10.21256/zhaw-3989.