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  Spatial control of lipid droplet proteins by the ERAD ubiquitin ligase Doa10

Ruggiano, A., Mora, G., Buxo, L., & Carvalho, P. (2016). Spatial control of lipid droplet proteins by the ERAD ubiquitin ligase Doa10. The EMBO Journal, 35(15), 1644-1655. doi:10.15252/embj.201593106.

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 Creators:
Ruggiano, Annamaria1, Author              
Mora, Gabriel2, Author
Buxo, Laura2, Author
Carvalho, Pedro2, Author
Affiliations:
1Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              
2external, ou_persistent22              

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Free keywords: INNER NUCLEAR-MEMBRANE; YEAST SACCHAROMYCES-CEREVISIAE; TAIL-ANCHORED PROTEINS; ENDOPLASMIC-RETICULUM; QUALITY-CONTROL; MISLOCALIZED PROTEINS; DEGRADATION; COMPLEX; GENE; PATHWAYBiochemistry & Molecular Biology; Cell Biology; Doa10; endoplasmic reticulum; ERAD; lipid droplets; protein degradation;
 Abstract: The endoplasmic reticulum (ER) plays a central role in the biogenesis of most membrane proteins. Among these are proteins localized to the surface of lipid droplets (LDs), fat storage organelles delimited by a phospholipid monolayer. The LD monolayer is often continuous with the membrane of the ER allowing certain membrane proteins to diffuse between the two organelles. In these connected organelles, how some proteins concentrate specifically at the surface of LDs is not known. Here, we show that the ERAD ubiquitin ligase Doa10 controls the levels of some LD proteins. Their degradation is dependent on the localization to the ER and appears independent of the folding state. Moreover, we show that by degrading the ER pool of these LD proteins, ERAD contributes to restrict their localization to LDs. The signals for LD targeting and Doa10-mediated degradation overlap, indicating that these are competing events. This spatial control of protein localization is a novel function of ERAD that might contribute to generate functional diversity in a continuous membrane system.

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Language(s): eng - English
 Dates: 2016-06-292016-08-01
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000380968100006
DOI: 10.15252/embj.201593106
 Degree: -

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Title: The EMBO Journal
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 35 (15) Sequence Number: - Start / End Page: 1644 - 1655 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1