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Published online
doi:10.1083/jcb.200811081
The Journal of Cell Biology, Vol. 185, No. 7, 1227-1242
The Rockefeller University Press, 0021-9525 $30.00
© Fröhlich et al.
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Article

A genome-wide screen for genes affecting eisosomes reveals Nce102 function in sphingolipid signaling



Florian Fröhlich1, Karen Moreira3, Pablo S. Aguilar4, Nina C. Hubner2, Matthias Mann2, Peter Walter3,5, and Tobias C. Walther1

1 Organelle Architecture and Dynamics and 2 Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
3 Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158
4 Institute Pasteur, CP 11400 Montevideo, Uruguay
5 Howard Hughes Medical Institute, San Francisco, CA 94158

Correspondence to Tobias C. Walther: twalther{at}biochem.mpg.de

The protein and lipid composition of eukaryotic plasma membranes is highly dynamic and regulated according to need. The sphingolipid-responsive Pkh kinases are candidates for mediating parts of this regulation, as they affect a diverse set of plasma membrane functions, such as cortical actin patch organization, efficient endocytosis, and eisosome assembly. Eisosomes are large protein complexes underlying the plasma membrane and help to sort a group of membrane proteins into distinct domains. In this study, we identify Nce102 in a genome-wide screen for genes involved in eisosome organization and Pkh kinase signaling. Nce102 accumulates in membrane domains at eisosomes where Pkh kinases also localize. The relative abundance of Nce102 in these domains compared with the rest of the plasma membrane is dynamically regulated by sphingolipids. Furthermore, Nce102 inhibits Pkh kinase signaling and is required for plasma membrane organization. Therefore, Nce102 might act as a sensor of sphingolipids that regulates plasma membrane function.

F. Fröhlich and K. Moreira contributed equally to this paper.

Abbreviations used in this paper: LC, liquid chromatography; MCC, membrane compartment occupied by Can1; MCP, membrane compartment occupied by Pma1; MS, mass spectrometry; PHS, phytosphingosine; SILAC, stable isotope labeling by amino acids in cell culture; TAP, tandem affinity purification.

© 2009 Fröhlich et al.
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