Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids

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

Standard

Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. / Valls, L A; Winther, Jakob R.; Stevens, T H.

In: Journal of Cell Biology, Vol. 111, No. 2, 1990, p. 361-8.

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

Harvard

Valls, LA, Winther, JR & Stevens, TH 1990, 'Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids', Journal of Cell Biology, vol. 111, no. 2, pp. 361-8.

APA

Valls, L. A., Winther, J. R., & Stevens, T. H. (1990). Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. Journal of Cell Biology, 111(2), 361-8.

Vancouver

Valls LA, Winther JR, Stevens TH. Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. Journal of Cell Biology. 1990;111(2):361-8.

Author

Valls, L A ; Winther, Jakob R. ; Stevens, T H. / Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. In: Journal of Cell Biology. 1990 ; Vol. 111, No. 2. pp. 361-8.

Bibtex

@article{127e761adf02469aa93c18c372ad70b3,
title = "Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids",
abstract = "The amino-terminal propeptide of carboxypeptidase Y (CPY) is necessary and sufficient for targeting this glycoprotein to the vacuole of Saccharomyces cerevisiae. A 16 amino acid stretch of the propeptide was subjected to region-directed mutagenesis using randomized oligonucleotides. Mutations altering any of four contiguous amino acids, Gln-Arg-Pro-Leu, resulted in secretion of the encoded CPY precursor (proCPY), demonstrating that these residues form the core of the vacuolar targeting signal. Cells that simultaneously synthesize both wild-type and sorting-defective forms of proCPY efficiently sort and deliver only the wild-type molecule to the vacuole. These results indicate that the PRC1 missorting mutations are cis-dominant, implying that the mutant forms of proCPY are secreted as a consequence of failing to interact with the sorting apparatus, rather than a general poisoning of the vacuolar protein targeting system.",
keywords = "Amino Acid Sequence, Base Sequence, Carboxypeptidases, Cathepsin A, Cloning, Molecular, Enzyme Precursors, Genes, Fungal, Glycoproteins, Molecular Sequence Data, Mutation, Oligonucleotide Probes, Phenotype, Protein Processing, Post-Translational, Restriction Mapping, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vacuoles",
author = "Valls, {L A} and Winther, {Jakob R.} and Stevens, {T H}",
year = "1990",
language = "English",
volume = "111",
pages = "361--8",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "2",

}

RIS

TY - JOUR

T1 - Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids

AU - Valls, L A

AU - Winther, Jakob R.

AU - Stevens, T H

PY - 1990

Y1 - 1990

N2 - The amino-terminal propeptide of carboxypeptidase Y (CPY) is necessary and sufficient for targeting this glycoprotein to the vacuole of Saccharomyces cerevisiae. A 16 amino acid stretch of the propeptide was subjected to region-directed mutagenesis using randomized oligonucleotides. Mutations altering any of four contiguous amino acids, Gln-Arg-Pro-Leu, resulted in secretion of the encoded CPY precursor (proCPY), demonstrating that these residues form the core of the vacuolar targeting signal. Cells that simultaneously synthesize both wild-type and sorting-defective forms of proCPY efficiently sort and deliver only the wild-type molecule to the vacuole. These results indicate that the PRC1 missorting mutations are cis-dominant, implying that the mutant forms of proCPY are secreted as a consequence of failing to interact with the sorting apparatus, rather than a general poisoning of the vacuolar protein targeting system.

AB - The amino-terminal propeptide of carboxypeptidase Y (CPY) is necessary and sufficient for targeting this glycoprotein to the vacuole of Saccharomyces cerevisiae. A 16 amino acid stretch of the propeptide was subjected to region-directed mutagenesis using randomized oligonucleotides. Mutations altering any of four contiguous amino acids, Gln-Arg-Pro-Leu, resulted in secretion of the encoded CPY precursor (proCPY), demonstrating that these residues form the core of the vacuolar targeting signal. Cells that simultaneously synthesize both wild-type and sorting-defective forms of proCPY efficiently sort and deliver only the wild-type molecule to the vacuole. These results indicate that the PRC1 missorting mutations are cis-dominant, implying that the mutant forms of proCPY are secreted as a consequence of failing to interact with the sorting apparatus, rather than a general poisoning of the vacuolar protein targeting system.

KW - Amino Acid Sequence

KW - Base Sequence

KW - Carboxypeptidases

KW - Cathepsin A

KW - Cloning, Molecular

KW - Enzyme Precursors

KW - Genes, Fungal

KW - Glycoproteins

KW - Molecular Sequence Data

KW - Mutation

KW - Oligonucleotide Probes

KW - Phenotype

KW - Protein Processing, Post-Translational

KW - Restriction Mapping

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Vacuoles

M3 - Journal article

C2 - 2199455

VL - 111

SP - 361

EP - 368

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 2

ER -

ID: 43974603