Review: biosynthesis and function of yeast vacuolar proteases

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

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Review : biosynthesis and function of yeast vacuolar proteases. / Van Den Hazel, H B; Kielland-Brandt, Morten; Winther, Jakob R.

In: Yeast (Chichester, England), Vol. 12, No. 1, 1996, p. 1-16.

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

Harvard

Van Den Hazel, HB, Kielland-Brandt, M & Winther, JR 1996, 'Review: biosynthesis and function of yeast vacuolar proteases', Yeast (Chichester, England), vol. 12, no. 1, pp. 1-16. https://doi.org/10.1002/(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N

APA

Van Den Hazel, H. B., Kielland-Brandt, M., & Winther, J. R. (1996). Review: biosynthesis and function of yeast vacuolar proteases. Yeast (Chichester, England), 12(1), 1-16. https://doi.org/10.1002/(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N

Vancouver

Van Den Hazel HB, Kielland-Brandt M, Winther JR. Review: biosynthesis and function of yeast vacuolar proteases. Yeast (Chichester, England). 1996;12(1):1-16. https://doi.org/10.1002/(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N

Author

Van Den Hazel, H B ; Kielland-Brandt, Morten ; Winther, Jakob R. / Review : biosynthesis and function of yeast vacuolar proteases. In: Yeast (Chichester, England). 1996 ; Vol. 12, No. 1. pp. 1-16.

Bibtex

@article{05ddcbcb05cd47e0b0bb872f5e94948e,
title = "Review: biosynthesis and function of yeast vacuolar proteases",
abstract = "The yeast vacuole, which is equivalent to the lysosome of higher eukaryotes, is one of the best characterized degradative organelles. This review describes the biosynthesis and function of yeast vacuolar proteases. Most of these enzymes are delivered to the vacuole via the early compartments of the secretory pathway and the endosome, while one of them is directly imported from the cytoplasm. The proteases are synthesized as precursors which undergo many post-translational modifications before the final active form is generated. Proteolytic activation by developments in the analysis of the functions of vacuolar proteolysis are described. Substrates of the vacuolar proteases are mostly imported via endocytosis or autophagocytosis, and vacuolar proteolysis appears to be mainly important under nutritional stress conditions and sporulation.",
keywords = "Amino Acid Sequence, Biological Transport, Active, Endocytosis, Endopeptidases, Enzyme Activation, Enzyme Precursors, Molecular Sequence Data, Saccharomyces cerevisiae, Substrate Specificity, Vacuoles, Yeasts",
author = "{Van Den Hazel}, {H B} and Morten Kielland-Brandt and Winther, {Jakob R.}",
year = "1996",
doi = "10.1002/(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N",
language = "English",
volume = "12",
pages = "1--16",
journal = "Yeast",
issn = "0749-503X",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Review

T2 - biosynthesis and function of yeast vacuolar proteases

AU - Van Den Hazel, H B

AU - Kielland-Brandt, Morten

AU - Winther, Jakob R.

PY - 1996

Y1 - 1996

N2 - The yeast vacuole, which is equivalent to the lysosome of higher eukaryotes, is one of the best characterized degradative organelles. This review describes the biosynthesis and function of yeast vacuolar proteases. Most of these enzymes are delivered to the vacuole via the early compartments of the secretory pathway and the endosome, while one of them is directly imported from the cytoplasm. The proteases are synthesized as precursors which undergo many post-translational modifications before the final active form is generated. Proteolytic activation by developments in the analysis of the functions of vacuolar proteolysis are described. Substrates of the vacuolar proteases are mostly imported via endocytosis or autophagocytosis, and vacuolar proteolysis appears to be mainly important under nutritional stress conditions and sporulation.

AB - The yeast vacuole, which is equivalent to the lysosome of higher eukaryotes, is one of the best characterized degradative organelles. This review describes the biosynthesis and function of yeast vacuolar proteases. Most of these enzymes are delivered to the vacuole via the early compartments of the secretory pathway and the endosome, while one of them is directly imported from the cytoplasm. The proteases are synthesized as precursors which undergo many post-translational modifications before the final active form is generated. Proteolytic activation by developments in the analysis of the functions of vacuolar proteolysis are described. Substrates of the vacuolar proteases are mostly imported via endocytosis or autophagocytosis, and vacuolar proteolysis appears to be mainly important under nutritional stress conditions and sporulation.

KW - Amino Acid Sequence

KW - Biological Transport, Active

KW - Endocytosis

KW - Endopeptidases

KW - Enzyme Activation

KW - Enzyme Precursors

KW - Molecular Sequence Data

KW - Saccharomyces cerevisiae

KW - Substrate Specificity

KW - Vacuoles

KW - Yeasts

U2 - 10.1002/(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N

DO - 10.1002/(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N

M3 - Journal article

C2 - 8789256

VL - 12

SP - 1

EP - 16

JO - Yeast

JF - Yeast

SN - 0749-503X

IS - 1

ER -

ID: 43974274