Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae.

Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae. Abstract Text:

N Nakamura,A Matsuura,Y Wada,Y Ohsumi,

Acidification inside vacuoles has been shown to play a key role in a number of physiologically important cellular events. We studied the role of vacuolar membrane H(+)-ATPase in the autophagic process of Saccharomyces cerevisiae. Mutants lacking VMA genes which encode their subunits of the vacuolar H(+)-ATPase accumulated autophagic bodies in vacuoles on starvation. vma mutants also had a defect in protein degradation induced by starvation. In vma mutants, the activities of vacuolar proteases were remarkably lower than those of the wild-type. Overexpression of vacuolar proteases did not overcome the defect in the disintegration of autophagic bodies in vma mutant, even the overexpressed proteinase A and proteinase B being substantially localized to the vacuolar compartment and undergoing proper proteolytic maturation. Our results showed that the acidification of vacuoles is not required for the formation and delivery of autophagosomes to vacuoles, but is essential for the disintegration of autophagic bodies.

Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae. Publishing Authors By Initials

N Nakamura,A Matsuura,Y Wada,Y Ohsumi,

For similar cells: cellular structures: intracellular space: cytoplasm: cytoplasmic structures: organelles: cytoplasmic vesicles: vacuoles research abstracts see: cells: cellular structures: intracellular space: cytoplasm: cytoplasmic structures: organelles: cytoplasmic vesicles: vacuoles research

PUBMED ID PMID:

MEDLINE DATE:

Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 121

Page Numbers: 338-44

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1997

Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae. Keywords Mesh Terms:

KEYWORDS: Vacuoles

MESH TERMS: enzymology

Chemical & Substance for Abstract: Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae. Information

Substance Name: Proton-Translocating ATPases

Registry Number: EC 3.6.3.14

Grant and Affiliation Information for Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae.

AFFILIATION: Department of Biology, Graduate School of Arts and Sciences, University of Tokyo.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae Related Publications

• A new powder diffractometer for synchrotron radiation with a multiple-detector system.
• Acidification of vacuoles is required for autophagic degradation in the yeast, Saccharomyces cerevisiae.
• Dynamics and function of PtdIns(3)P in autophagy.
• Lipidation of Atg8: How is substrate specificity determined without a canonical E3 enzyme?
• Long Horizontal Parallel Slits with 0.03 degrees Angular Resolution for Powder Diffraction Using Synchrotron Radiation.
• Organization of the Pre-autophagosomal Structure Responsible for Autophagosome Formation.
• Physiological pH and Acidic Phospholipids Contribute to Substrate Specificity in Lipidation of Atg8.
• Sigmoid colon diverticulosis adherent to mesh plug migration after open inguinal hernia repair.
• Starved cells eat ribosomes.
• The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy.
• The Atg18-Atg2 Complex Is Recruited to Autophagic Membranes via Phosphatidylinositol 3-Phosphate and Exerts an Essential Function.
• Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast.
• Transport of phosphatidylinositol 3-phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae.
• [Key questions about membrane dynamics during autophagy]
• [Molecular mechanisms for meiotic arrest that is canceled by fertilization in vertebrate eggs]