Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae

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Standard

Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. / Jørgensen, Marianne U.; Emr, Scott D.; Winther, Jakob R.

In: European Journal of Biochemistry, Vol. 260, No. 2, 1999, p. 461-469.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jørgensen, MU, Emr, SD & Winther, JR 1999, 'Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae', European Journal of Biochemistry, vol. 260, no. 2, pp. 461-469. https://doi.org/10.1046/j.1432-1327.1999.00176.x

APA

Jørgensen, M. U., Emr, S. D., & Winther, J. R. (1999). Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. European Journal of Biochemistry, 260(2), 461-469. https://doi.org/10.1046/j.1432-1327.1999.00176.x

Vancouver

Jørgensen MU, Emr SD, Winther JR. Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. European Journal of Biochemistry. 1999;260(2):461-469. https://doi.org/10.1046/j.1432-1327.1999.00176.x

Author

Jørgensen, Marianne U. ; Emr, Scott D. ; Winther, Jakob R. / Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. In: European Journal of Biochemistry. 1999 ; Vol. 260, No. 2. pp. 461-469.

Bibtex

@article{f7b93e8665314db3b0fc1d82f2980ba2,
title = "Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae",
abstract = "Vp10p is a receptor that sorts several different vacuolar proteins by cycling between a late Golgi compartment and the endosome. The cytoplasmic tail of Vps10p is necessary for the recycling, whereas the lumenal domain is predicted to interact with the soluble ligands. We have studied ligand binding to Vps10p by introducing deletions in the lumenal region. This region contains two domains with homology to each other. Domain 2 binds carboxypeptidase Y (CPY), proteinase A (PrA) and hybrids of these proteases with invertase. Moreover, we show that aminopeptidase Y (APY) is a ligand of Vps10p. The native proteases compete for binding to domain 2. Binding of CPY(156)-invertase or PrA(137)-invertase, on the other hand, do not interfere with binding of CPY to Vps10p. Furthermore, the Q24RPL27 sequence known to be important for vacuolar sorting of CPY, is of little importance in the Vps10p-dependent sorting of CPY-invertase. Apparently, domain 2 contains two different binding sites; one for APY, CPY and PrA, and one for CPY-invertase and PrA-invertase. The latter interaction seems not to be sequence specific, and we suggest that an unfolded structure in these ligands is recognized by Vps10p.",
keywords = "Aminopeptidases, Aspartic Acid Endopeptidases, Biological Transport, Carboxypeptidases, Cathepsin A, Escherichia coli, Fungal Proteins, Glycoside Hydrolases, Ligands, Polymerase Chain Reaction, Protein Folding, Receptors, Cell Surface, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vacuoles, Vesicular Transport Proteins, beta-Fructofuranosidase",
author = "J{\o}rgensen, {Marianne U.} and Emr, {Scott D.} and Winther, {Jakob R.}",
year = "1999",
doi = "10.1046/j.1432-1327.1999.00176.x",
language = "English",
volume = "260",
pages = "461--469",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Springer Verlag",
number = "2",

}

RIS

TY - JOUR

T1 - Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae

AU - Jørgensen, Marianne U.

AU - Emr, Scott D.

AU - Winther, Jakob R.

PY - 1999

Y1 - 1999

N2 - Vp10p is a receptor that sorts several different vacuolar proteins by cycling between a late Golgi compartment and the endosome. The cytoplasmic tail of Vps10p is necessary for the recycling, whereas the lumenal domain is predicted to interact with the soluble ligands. We have studied ligand binding to Vps10p by introducing deletions in the lumenal region. This region contains two domains with homology to each other. Domain 2 binds carboxypeptidase Y (CPY), proteinase A (PrA) and hybrids of these proteases with invertase. Moreover, we show that aminopeptidase Y (APY) is a ligand of Vps10p. The native proteases compete for binding to domain 2. Binding of CPY(156)-invertase or PrA(137)-invertase, on the other hand, do not interfere with binding of CPY to Vps10p. Furthermore, the Q24RPL27 sequence known to be important for vacuolar sorting of CPY, is of little importance in the Vps10p-dependent sorting of CPY-invertase. Apparently, domain 2 contains two different binding sites; one for APY, CPY and PrA, and one for CPY-invertase and PrA-invertase. The latter interaction seems not to be sequence specific, and we suggest that an unfolded structure in these ligands is recognized by Vps10p.

AB - Vp10p is a receptor that sorts several different vacuolar proteins by cycling between a late Golgi compartment and the endosome. The cytoplasmic tail of Vps10p is necessary for the recycling, whereas the lumenal domain is predicted to interact with the soluble ligands. We have studied ligand binding to Vps10p by introducing deletions in the lumenal region. This region contains two domains with homology to each other. Domain 2 binds carboxypeptidase Y (CPY), proteinase A (PrA) and hybrids of these proteases with invertase. Moreover, we show that aminopeptidase Y (APY) is a ligand of Vps10p. The native proteases compete for binding to domain 2. Binding of CPY(156)-invertase or PrA(137)-invertase, on the other hand, do not interfere with binding of CPY to Vps10p. Furthermore, the Q24RPL27 sequence known to be important for vacuolar sorting of CPY, is of little importance in the Vps10p-dependent sorting of CPY-invertase. Apparently, domain 2 contains two different binding sites; one for APY, CPY and PrA, and one for CPY-invertase and PrA-invertase. The latter interaction seems not to be sequence specific, and we suggest that an unfolded structure in these ligands is recognized by Vps10p.

KW - Aminopeptidases

KW - Aspartic Acid Endopeptidases

KW - Biological Transport

KW - Carboxypeptidases

KW - Cathepsin A

KW - Escherichia coli

KW - Fungal Proteins

KW - Glycoside Hydrolases

KW - Ligands

KW - Polymerase Chain Reaction

KW - Protein Folding

KW - Receptors, Cell Surface

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Vacuoles

KW - Vesicular Transport Proteins

KW - beta-Fructofuranosidase

U2 - 10.1046/j.1432-1327.1999.00176.x

DO - 10.1046/j.1432-1327.1999.00176.x

M3 - Journal article

C2 - 10095782

VL - 260

SP - 461

EP - 469

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 2

ER -

ID: 43973970