The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting.

The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting. Research Abstract Details 

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The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting. Abstract Text:

Ju Huang,Fulvio Reggiori,Daniel J Klionsky,

Trehalose serves as a storage source of carbon and plays important roles under various stress conditions. For example, in many organisms trehalose has a critical function in preserving membrane structure and fluidity during dehydration/rehydration. In the yeast Saccharomyces cerevisiae, trehalose accumulates in the cell when the nutrient supply is limited but is rapidly degraded when the supply of nutrients is renewed. Hydrolysis of trehalose in yeast depends on neutral trehalase and acid trehalase (Ath1). Ath1 resides and functions in the vacuole; however, it appears to catalyze the hydrolysis of extracellular trehalose. Little is known about the transport route of Ath1 to the vacuole or how it encounters its substrate. Here, through the use of various trafficking mutants we showed that this hydrolase reaches its final destination through the multivesicular body (MVB) pathway. In contrast to the vast majority of proteins sorted into this pathway, Ath1 does not require ubiquitination for proper localization. Mutagenesis analyses aimed at identifying the unknown targeting signal revealed that the transmembrane domain of Ath1 contains the information sufficient for its selective sequestration into MVB internal vesicles.

The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting. Publishing Authors By Initials

J Huang,F Reggiori,DJ Klionsky,

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

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The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Molecular biology of the cell

VOLUME: 18

Page Numbers: 2511-24

Journal Abbreviation: Mol. Biol. Cell

ISSN: 1059-1524

DAY: 2

MONTH: 05

YEAR: 2007

The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting. Information

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LANGUAGE: eng

NlmUniqueID: 9201390

The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting. Keywords Mesh Terms:

KEYWORDS: Vacuoles

MESH TERMS: enzymology

Chemical & Substance for Abstract: The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting. Information

Substance Name: Ubiquitin

Registry Number: 0

Grant and Affiliation Information for The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting.

AFFILIATION: Life Sciences Institute, Department of Molecular, University of Michigan, Ann Arbor, MI 48109, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM53396

ACRONYM: GM

MEDLINETA: Mol Biol Cell

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