Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein.

Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Abstract Text:

Yang Cao,Daniel J Klionsky,Yang Cao,Daniel J Klionsky,

The most striking morphological feature of eukaryotic cells is the presence of various membrane-enclosed compartments. These compartments, including organelles and transient transport intermediates, are not static. Rather, dynamic exchange of proteins and membrane is needed to maintain cellular homeostasis. One of the most dramatic examples of membrane mobilization is seen during the process of macroautophagy. Macroautophagy is the primary cellular pathway for degradation of long-lived proteins and organelles. In response to environmental cues, such as starvation or other types of stress, the cell produces a unique membrane structure, the phagophore. The phagophore sequesters cytoplasm as it forms a double-membrane cytosolic vesicle, an autophagosome. Upon completion, the autophagosome fuses with a lysosome or a vacuole in yeast, which delivers hydrolases that break down the inner autophagosome membrane along with its cargo, and the resulting macromolecules are released back into the cytosol for reuse. Autophagy is therefore a recycling process, allowing cells to survive periods of nutrient limitation; however, it has a wider physiological role, participating in development and aging, and also in protection against pathogen invasion, cancer and certain neurodegenerative diseases. In many cases, the role of autophagy is identified through studies of an autophagy-related protein, Atg6/Beclin 1. This protein is part of a lipid kinase complex, and recent studies suggest that it plays a central role in coordinating the cytoprotective function of autophagy and in opposing the cellular death process of apoptosis. Here, we summarize our current knowledge of Atg6/Beclin 1 in different model organisms and its unique function in the cell.

Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Publishing Authors By Initials

Y Cao,DJ Klionsky,Y Cao,DJ Klionsky,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Journal Published:

PUBLICATION TYPE: Review

Journal: Cell research

VOLUME: 17

Page Numbers: 839-49

Journal Abbreviation: Cell Res.

ISSN: 1748-7838

DAY: 15

MONTH: Oct

YEAR: 2007

Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Information

Number of References: 88

LANGUAGE: eng

NlmUniqueID: 9425763

Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein.

AFFILIATION: Department of Molecular, Cellular and Developmental Biology, Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109-2216, USA.

Country: China

AGENCY: United States NIGMS

GRANT: GM53396

ACRONYM: GM

MEDLINETA: Cell Res

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein Related Publications

• A cycling protein complex required for selective autophagy.
• Analysis of autophagosome membrane cycling by fluorescence microscopy.
• Arp2 links autophagic machinery with the actin cytoskeleton.
• Atg22 recycles amino acids to link the degradative and recycling functions of autophagy.
• Atg27 is required for autophagy-dependent cycling of Atg9.
• Atg8 Controls Phagophore Expansion during Autophagosome Formation.
• Autophagosome formation: core machinery and adaptations.
• Autophagy and human disease.
• Autophagy fights disease through cellular self-digestion.
• Autophagy revisited: a conversation with Christian de Duve.
• Dissecting autophagosome formation: The missing pieces.
• Dual role of Atg1 in regulation of autophagy-specific PAS assembly in Saccharomyces cerevisiae.
• Eating the endoplasmic reticulum: quality control by autophagy.
• Getting into the flow.
• Harpooning the Cvt complex to the phagophore assembly site.
• How cells clean house.
• How to live long and prosper: autophagy, mitochondria, and aging.
• How we do business (or, why does it take other journals so long to review your paper?).
• In vivo reconstitution of autophagy in Saccharomyces cerevisiae.
• Monitoring Autophagy in Yeast: The Pho8Delta60 Assay.
• Nonclassical protein sorting.
• Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein.
• Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae.
• Protein turnover via autophagy: implications for metabolism.
• Quantitative analysis of autophagy-related protein stoichiometry by fluorescence microscopy.
• Quantitative regulation of vesicle formation in yeast nonspecific autophagy.
• Recruitment of Atg9 to the preautophagosomal structure by Atg11 is essential for selective autophagy in budding yeast.
• The Atg1 Kinase Complex Is Involved in the Regulation of Protein Recruitment to Initiate Sequestering Vesicle Formation for Nonspecific Autophagy in Saccharomyces cerevisiae.
• The quiz factor.
• The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting.