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J. Biol. Chem., Vol. 279, Issue 22, 23699-23709, May 28, 2004
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Association of Stomatin with Lipid Bodies*
**
From the
Institute of Biochemistry, Medical University of Vienna, and Mass Spectrometry Unit, University of Vienna, Vienna Biocenter, Vienna A-1030, Austria, ¶Institute for Biophysics, Johannes Kepler University, Linz A-4040, Austria, and ||Institute for Molecular Bioscience, Centre for Microscopy and Microanalysis, University of Queensland, Queensland 4072, Australia
The oligomeric lipid raft-associated integral protein stomatin normally localizes to the plasma membrane and the late endosomal compartment. Similar to the caveolins, it is targeted to lipid bodies (LBs) on overexpression. Endogenous stomatin also associates with LBs to a small extent. Green fluorescent protein-tagged stomatin (StomGFP) and the dominant-negative caveolin-3 mutant DGV(cav3)HA occupy distinct domains on LB surfaces but eventually intermix. Studies of StomGFP deletion mutants reveal that the region for membrane association but not oligomerization and raft association is essential for LB targeting. Blocking protein synthesis leads to the redistribution of StomGFP from LBs to LysoTracker-positive vesicles indicating a connection with the late endosomal/lysosomal pathway. Live microscopy of StomGFP reveals multiple interactions between LBs and microtubule-associated vesicles possibly representing signaling events and/or the exchange of cargo. Proteomic analysis of isolated LBs identifies adipophilin and TIP47, various lipid-specific enzymes, cytoskeletal components, chaperones, Ras-related proteins, protein kinase D2, and other regulatory proteins. The association of the Rab proteins 1, 6, 7, 10, and 18 with LBs indicates various connections to other compartments. Our data suggest that LBs are not only involved in the storage of lipids but also participate actively in the cellular signaling network and the homeostasis of lipids.
Received for publication, September 24, 2003 , and in revised form, February 19, 2004.
* This work was supported by grants from the Austrian Science Fund (FWF). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
** To whom correspondence should be addressed: Institute of Biochemistry, MFPL, Medical University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9/3, Vienna A-1030, Austria. Tel.: 43-1-4277-61660; Fax: 43-1-4277-9616; E-mail: rainer.prohaska{at}univie.ac.at.
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