English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The evolutionarily conserved protein CG9186 is associated with lipid droplets, required for their positioning and for fat storage.

Thiel, K., Heier, C., Haberl, V., Thul, P. J., Oberer, M., Lass, A., et al. (2013). The evolutionarily conserved protein CG9186 is associated with lipid droplets, required for their positioning and for fat storage. Journal of Cell Science, 126(10), 2198-2212. doi:10.1242/jcs.120493.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-16FA-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-27F2-5
Genre: Journal Article

Files

show Files
hide Files
:
1819370.pdf (Publisher version), 7MB
Name:
1819370.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1819370_Supplement_1.pdf (Supplementary material), 680KB
Name:
1819370_Supplement_1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Thiel, K.1, Author              
Heier, C., Author
Haberl, V., Author
Thul, P. J.1, Author              
Oberer, M., Author
Lass, A., Author
Jäckle, H.1, Author              
Beller, M.1, Author              
Affiliations:
1Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society, ou_578590              

Content

show
hide
Free keywords: Lipid droplets, Organelle clustering, Organelle positioning, Lipid metabolism, Drosophila melanogaster
 Abstract: Lipid droplets (LDs) are specialized cell organelles for the storage of energy-rich lipids. Although lipid storage is a conserved feature of all cells and organisms, little is known about fundamental aspects of the cell biology of LDs, including their biogenesis, structural assembly and subcellular positioning, and the regulation of organismic energy homeostasis. We identified a novel LD-associated protein family, represented by the Drosophila protein CG9186 and its murine homolog MGI:1916082. In the absence of LDs, both proteins localize at the endoplasmic reticulum (ER). Upon lipid storage induction, they translocate to LDs using an evolutionarily conserved targeting mechanism that acts through a 60-amino-acid targeting motif in the center of the CG9186 protein. Overexpression of CG9186, and MGI: 1916082, causes clustering of LDs in both tissue culture and salivary gland cells, whereas RNAi knockdown of CG9186 results in a reduction of LDs. Organismal RNAi knockdown of CG9186 results in a reduction in lipid storage levels of the fly. The results indicate that we identified the first members of a novel and evolutionarily conserved family of lipid storage regulators, which are also required to properly position LDs within cells.

Details

show
hide
Language(s): eng - English
 Dates: 2013-05-15
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1242/jcs.120493
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Cell Science
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 126 (10) Sequence Number: - Start / End Page: 2198 - 2212 Identifier: -