NCU-G1 is a highly glycosylated integral membrane protein of the lysosome.

Schieweck O, Damme M, Schröder B, Hasilik A, Schmidt B, Lübke T (2009)
Biochemical Journal 422(1): 83-90.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
Schieweck, Oliver; Damme, MarkusUniBi; Schröder, Bernd; Hasilik, Andrey; Schmidt, Bernhard; Lübke, TorbenUniBi
Abstract / Bemerkung
Until recently, a modest number of approx. 40 lysosomal membrane proteins had been identified and even fewer were characterized in their function. In a proteomic study, using lysosomal membranes from human placenta we identified several candidate lysosomal membrane proteins and proved the lysosomal localization of two of them. In the present study, we demonstrate the lysosomal localization of the mouse orthologue of the human C1orf85 protein, which has been termed kidney-predominant protein NCU-G1 (GenBank accession number: AB027141). NCU-G1 encodes a 404 amino acid protein with a calculated molecular mass of 39 kDa. The bioinformatics analysis of its amino acid sequence suggests it is a type I transmembrane protein containing a single tyrosine-based consensus lysosomal sorting motif at position 400 within the 12-residue C-terminal tail. Its lysosomal localization was confirmed using immunofluorescence with a C-terminally His-tagged NCU-G1 and the lysosomal marker LAMP-1 (lysosome-associated membrane protein-1) as a reference, and by subcellular fractionation of mouse liver after a tyloxapol-induced density shift of the lysosomal fraction using an anti-NCU-G1 antiserum. In transiently transfected HT1080 and HeLa cells, the His-tagged NCU-G1 was detected in two molecular forms with apparent protein sizes of 70 and 80 kDa, and in mouse liver the endogenous wild-type NCU-G1 was detected as a 75 kDa protein. The remarkable difference between the apparent and the calculated molecular masses of NCU-G1 was shown, by digesting the protein with N-glycosidase F, to be due to an extensive glycosylation. The lysosomal localization was impaired by mutational replacement of an alanine residue for the tyrosine residue within the putative sorting motif.
Erscheinungsjahr
2009
Zeitschriftentitel
Biochemical Journal
Band
422
Ausgabe
1
Seite(n)
83-90
ISSN
0264-6021
eISSN
1470-8728
Page URI
https://pub.uni-bielefeld.de/record/1902143

Zitieren

Schieweck O, Damme M, Schröder B, Hasilik A, Schmidt B, Lübke T. NCU-G1 is a highly glycosylated integral membrane protein of the lysosome. Biochemical Journal. 2009;422(1):83-90.
Schieweck, O., Damme, M., Schröder, B., Hasilik, A., Schmidt, B., & Lübke, T. (2009). NCU-G1 is a highly glycosylated integral membrane protein of the lysosome. Biochemical Journal, 422(1), 83-90. https://doi.org/10.1042/BJ20090567
Schieweck, O., Damme, M., Schröder, B., Hasilik, A., Schmidt, B., and Lübke, T. (2009). NCU-G1 is a highly glycosylated integral membrane protein of the lysosome. Biochemical Journal 422, 83-90.
Schieweck, O., et al., 2009. NCU-G1 is a highly glycosylated integral membrane protein of the lysosome. Biochemical Journal, 422(1), p 83-90.
O. Schieweck, et al., “NCU-G1 is a highly glycosylated integral membrane protein of the lysosome.”, Biochemical Journal, vol. 422, 2009, pp. 83-90.
Schieweck, O., Damme, M., Schröder, B., Hasilik, A., Schmidt, B., Lübke, T.: NCU-G1 is a highly glycosylated integral membrane protein of the lysosome. Biochemical Journal. 422, 83-90 (2009).
Schieweck, Oliver, Damme, Markus, Schröder, Bernd, Hasilik, Andrey, Schmidt, Bernhard, and Lübke, Torben. “NCU-G1 is a highly glycosylated integral membrane protein of the lysosome.”. Biochemical Journal 422.1 (2009): 83-90.

16 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Stat3-mediated alterations in lysosomal membrane protein composition.
Lloyd-Lewis B, Krueger CC, Sargeant TJ, D'Angelo ME, Deery MJ, Feret R, Howard JA, Lilley KS, Watson CJ., J Biol Chem 293(12), 2018
PMID: 29343516
Silicanin-1 is a conserved diatom membrane protein involved in silica biomineralization.
Kotzsch A, Gröger P, Pawolski D, Bomans PHH, Sommerdijk NAJM, Schlierf M, Kröger N., BMC Biol 15(1), 2017
PMID: 28738898
The Arabidopsis tonoplast is almost devoid of glycoproteins with complex N-glycans, unlike the rat lysosomal membrane.
Pedrazzini E, Caprera A, Fojadelli I, Stella A, Rocchetti A, Bassin B, Martinoia E, Vitale A., J Exp Bot 67(6), 2016
PMID: 26748395
Increased glucose utilization and decreased fatty acid metabolism in myotubes from Glmp(gt/gt) mice.
Kong XY, Feng YZ, Eftestøl E, Kase ET, Haugum H, Eskild W, Rustan AC, Thoresen GH., Arch Physiol Biochem 122(1), 2016
PMID: 26707125
Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease.
Peters J, Rittger A, Weisner R, Knabbe J, Zunke F, Rothaug M, Damme M, Berkovic SF, Blanz J, Saftig P, Schwake M., Biochem Biophys Res Commun 457(3), 2015
PMID: 25576872
Lack of the Lysosomal Membrane Protein, GLMP, in Mice Results in Metabolic Dysregulation in Liver.
Kong XY, Kase ET, Herskedal A, Schjalm C, Damme M, Nesset CK, Thoresen GH, Rustan AC, Eskild W., PLoS One 10(6), 2015
PMID: 26047317
Gene disruption of Mfsd8 in mice provides the first animal model for CLN7 disease.
Damme M, Brandenstein L, Fehr S, Jankowiak W, Bartsch U, Schweizer M, Hermans-Borgmeyer I, Storch S., Neurobiol Dis 65(), 2014
PMID: 24423645
Loss of lysosomal membrane protein NCU-G1 in mice results in spontaneous liver fibrosis with accumulation of lipofuscin and iron in Kupffer cells.
Kong XY, Nesset CK, Damme M, Løberg EM, Lübke T, Mæhlen J, Andersson KB, Lorenzo PI, Roos N, Thoresen GH, Rustan AC, Kase ET, Eskild W., Dis Model Mech 7(3), 2014
PMID: 24487409
An extended proteome map of the lysosomal membrane reveals novel potential transporters.
Chapel A, Kieffer-Jaquinod S, Sagné C, Verdon Q, Ivaldi C, Mellal M, Thirion J, Jadot M, Bruley C, Garin J, Gasnier B, Journet A., Mol Cell Proteomics 12(6), 2013
PMID: 23436907
Lysosomal membrane proteins and their central role in physiology.
Schwake M, Schröder B, Saftig P., Traffic 14(7), 2013
PMID: 23387372
TM7SF1 (GPR137B): a novel lysosome integral membrane protein.
Gao J, Xia L, Lu M, Zhang B, Chen Y, Xu R, Wang L., Mol Biol Rep 39(9), 2012
PMID: 22729905
Classification of subcellular location by comparative proteomic analysis of native and density-shifted lysosomes.
Della Valle MC, Sleat DE, Zheng H, Moore DF, Jadot M, Lobel P., Mol Cell Proteomics 10(4), 2011
PMID: 21252268
Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L.
Savalas LR, Gasnier B, Damme M, Lübke T, Wrocklage C, Debacker C, Jézégou A, Reinheckel T, Hasilik A, Saftig P, Schröder B., Biochem J 439(1), 2011
PMID: 21692750
The proteome of lysosomes.
Schröder BA, Wrocklage C, Hasilik A, Saftig P., Proteomics 10(22), 2010
PMID: 20957757
SID1 transmembrane family, member 2 (Sidt2): a novel lysosomal membrane protein.
Jialin G, Xuefan G, Huiwen Z., Biochem Biophys Res Commun 402(4), 2010
PMID: 20965152
A gene network regulating lysosomal biogenesis and function.
Sardiello M, Palmieri M, di Ronza A, Medina DL, Valenza M, Gennarino VA, Di Malta C, Donaudy F, Embrione V, Polishchuk RS, Banfi S, Parenti G, Cattaneo E, Ballabio A., Science 325(5939), 2009
PMID: 19556463

48 References

Daten bereitgestellt von Europe PubMed Central.

Proteomics of the lysosome.
Lubke T, Lobel P, Sleat DE., Biochim. Biophys. Acta 1793(4), 2008
PMID: 18977398

Saftig, 0
Molecular physiology and pathophysiology of lysosomal membrane transporters.
Sagne C, Gasnier B., J. Inherit. Metab. Dis. 31(2), 2008
PMID: 18425435

Ruivo, Biochim. Biophys. Acta 1793(), 2008
A novel gene encoding an integral membrane protein is mutated in nephropathic cystinosis.
Town M, Jean G, Cherqui S, Attard M, Forestier L, Whitmore SA, Callen DF, Gribouval O, Broyer M, Bates GP, van't Hoff W, Antignac C., Nat. Genet. 18(4), 1998
PMID: 9537412
A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases.
Verheijen FW, Verbeek E, Aula N, Beerens CE, Havelaar AC, Joosse M, Peltonen L, Aula P, Galjaard H, van der Spek PJ, Mancini GM., Nat. Genet. 23(4), 1999
PMID: 10581036
Identification of the gene causing mucolipidosis type IV.
Bargal R, Avidan N, Ben-Asher E, Olender Z, Zeigler M, Frumkin A, Raas-Rothschild A, Glusman G, Lancet D, Bach G., Nat. Genet. 26(1), 2000
PMID: 10973263
Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel.
Sun M, Goldin E, Stahl S, Falardeau JL, Kennedy JC, Acierno JS Jr, Bove C, Kaneski CR, Nagle J, Bromley MC, Colman M, Schiffmann R, Slaugenhaupt SA., Hum. Mol. Genet. 9(17), 2000
PMID: 11030752
Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism.
Rutsch F, Gailus S, Miousse IR, Suormala T, Sagne C, Toliat MR, Nurnberg G, Wittkampf T, Buers I, Sharifi A, Stucki M, Becker C, Baumgartner M, Robenek H, Marquardt T, Hohne W, Gasnier B, Rosenblatt DS, Fowler B, Nurnberg P., Nat. Genet. 41(2), 2009
PMID: 19136951
Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice.
Tanaka Y, Guhde G, Suter A, Eskelinen EL, Hartmann D, Lullmann-Rauch R, Janssen PM, Blanz J, von Figura K, Saftig P., Nature 406(6798), 2000
PMID: 10972293

Kornfeld, Ann. Rev. Cell Biol. 5(), 1989
LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase.
Reczek D, Schwake M, Schroder J, Hughes H, Blanz J, Jin X, Brondyk W, Van Patten S, Edmunds T, Saftig P., Cell 131(4), 2007
PMID: 18022370
Signals for sorting of transmembrane proteins to endosomes and lysosomes.
Bonifacino JS, Traub LM., Annu. Rev. Biochem. 72(), 2003
PMID: 12651740
Sorting of lysosomal proteins.
Braulke T, Bonifacino JS., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19046998
Leucine-based receptor sorting motifs are dependent on the spacing relative to the plasma membrane.
Geisler C, Dietrich J, Nielsen BL, Kastrup J, Lauritsen JP, Odum N, Christensen MD., J. Biol. Chem. 273(33), 1998
PMID: 9694892
Intracellular localization of p40, a protein identified in a preparation of lysosomal membranes.
Boonen M, Hamer I, Boussac M, Delsaute AF, Flamion B, Garin J, Jadot M., Biochem. J. 395(1), 2006
PMID: 16367739
TMEM74, a lysosome and autophagosome protein, regulates autophagy.
Yu C, Wang L, Lv B, Lu Y, Zeng L, Chen Y, Ma D, Shi T, Wang L., Biochem. Biophys. Res. Commun. 369(2), 2008
PMID: 18294959
Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome).
Hrebicek M, Mrazova L, Seyrantepe V, Durand S, Roslin NM, Noskova L, Hartmannova H, Ivanek R, Cizkova A, Poupetova H, Sikora J, Urinovska J, Stranecky V, Zeman J, Lepage P, Roquis D, Verner A, Ausseil J, Beesley CE, Maire I, Poorthuis BJ, van de Kamp J, van Diggelen OP, Wevers RA, Hudson TJ, Fujiwara TM, Majewski J, Morgan K, Kmoch S, Pshezhetsky AV., Am. J. Hum. Genet. 79(5), 2006
PMID: 17033958
The novel neuronal ceroid lipofuscinosis gene MFSD8 encodes a putative lysosomal transporter.
Siintola E, Topcu M, Aula N, Lohi H, Minassian BA, Paterson AD, Liu XQ, Wilson C, Lahtinen U, Anttonen AK, Lehesjoki AE., Am. J. Hum. Genet. 81(1), 2007
PMID: 17564970
Identification of the gene encoding the enzyme deficient in mucopolysaccharidosis IIIC (Sanfilippo disease type C).
Fan X, Zhang H, Zhang S, Bagshaw RD, Tropak MB, Callahan JW, Mahuran DJ., Am. J. Hum. Genet. 79(4), 2006
PMID: 16960811
Integral and associated lysosomal membrane proteins.
Schroder B, Wrocklage C, Pan C, Jager R, Kosters B, Schafer H, Elsasser HP, Mann M, Hasilik A., Traffic 8(12), 2007
PMID: 17897319
The two mannose 6-phosphate receptors transport distinct complements of lysosomal proteins.
Pohlmann R, Boeker MW, von Figura K., J. Biol. Chem. 270(45), 1995
PMID: 7592993
Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1.
Kollmann K, Damme M, Deuschl F, Kahle J, D'Hooge R, Lullmann-Rauch R, Lubke T., FEBS J. 276(5), 2009
PMID: 19187242
Identification of novel lysosomal matrix proteins by proteome analysis.
Kollmann K, Mutenda KE, Balleininger M, Eckermann E, von Figura K, Schmidt B, Lubke T., Proteomics 5(15), 2005
PMID: 16145712
Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency.
Lubke T, Marquardt T, Etzioni A, Hartmann E, von Figura K, Korner C., Nat. Genet. 28(1), 2001
PMID: 11326280
Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue.
DE DUVE C, PRESSMAN BC, GIANETTO R, WATTIAUX R, APPELMANS F., Biochem. J. 60(4), 1955
PMID: 13249955
[Effect of the injection of Triton WR 1339 on the hepatic lysosomes of the rat.]
WATTIAUX R, WIBO M, BAUDHUIN P., Arch. Int. Physiol. Biochim. 71(), 1963
PMID: 13999241
Targeted disruption of the M(r) 46,000 mannose 6-phosphate receptor gene in mice results in misrouting of lysosomal proteins.
Koster A, Saftig P, Matzner U, von Figura K, Peters C, Pohlmann R., EMBO J. 12(13), 1993
PMID: 8262064
Improved prediction of signal peptides: SignalP 3.0.
Bendtsen JD, Nielsen H, von Heijne G, Brunak S., J. Mol. Biol. 340(4), 2004
PMID: 15223320
Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes.
Krogh A, Larsson B, von Heijne G, Sonnhammer EL., J. Mol. Biol. 305(3), 2001
PMID: 11152613
Phagocytosis by rat liver: relationships between phagosomes and lysosomes.
Wattiaux R, Jadot M, Dubois F, Wattiaux-De Coninck S., Biochem. Biophys. Res. Commun. 220(3), 1996
PMID: 8607805
Demonstration of lysosomal localization for the mammalian ependymin-related protein using classical approaches combined with a novel density shift method.
Della Valle MC, Sleat DE, Sohar I, Wen T, Pintar JE, Jadot M, Lobel P., J. Biol. Chem. 281(46), 2006
PMID: 16954209
cDNA of a novel mRNA expressed predominantly in mouse kidney.
Kawamura T, Kuroda N, Kimura Y, Lazoura E, Okada N, Okada H., Biochem. Genet. 39(1-2), 2001
PMID: 11444019
Intracellular trafficking of lysosomal membrane proteins.
Hunziker W, Geuze HJ., Bioessays 18(5), 1996
PMID: 8639161
Mutations in the leucine zipper motif and sterol-sensing domain inactivate the Niemann-Pick C1 glycoprotein.
Watari H, Blanchette-Mackie EJ, Dwyer NK, Watari M, Neufeld EB, Patel S, Pentchev PG, Strauss JF 3rd., J. Biol. Chem. 274(31), 1999
PMID: 10419504
The targeting of cystinosin to the lysosomal membrane requires a tyrosine-based signal and a novel sorting motif.
Cherqui S, Kalatzis V, Trugnan G, Antignac C., J. Biol. Chem. 276(16), 2001
PMID: 11150305
Human NCU-G1 can function as a transcription factor and as a nuclear receptor co-activator.
Steffensen KR, Bouzga M, Skjeldal F, Kasi C, Karahasan A, Matre V, Bakke O, Guerin S, Eskild W., BMC Mol. Biol. 8(), 2007
PMID: 18021396
Lysosomes and autophagy in cell death control.
Kroemer G, Jaattela M., Nat. Rev. Cancer 5(11), 2005
PMID: 16239905
Cathepsin-regulated apoptosis.
Chwieralski CE, Welte T, Buhling F., Apoptosis 11(2), 2006
PMID: 16502253
Lysosomal serine protease CLN2 regulates tumor necrosis factor-alpha-mediated apoptosis in a Bid-dependent manner.
Autefage H, Albinet V, Garcia V, Berges H, Nicolau ML, Therville N, Altie MF, Caillaud C, Levade T, Andrieu-Abadie N., J. Biol. Chem. 284(17), 2009
PMID: 19246452
A gene network regulating lysosomal biogenesis and function.
Sardiello M, Palmieri M, di Ronza A, Medina DL, Valenza M, Gennarino VA, Di Malta C, Donaudy F, Embrione V, Polishchuk RS, Banfi S, Parenti G, Cattaneo E, Ballabio A., Science 325(5939), 2009
PMID: 19556463

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 19489740
PubMed | Europe PMC

Suchen in

Google Scholar