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MBC in Press, published online ahead of print January 30, 2008
Mol. Biol. Cell 10.1091/mbc.E07-10-1053

A more recent version of this article appeared on April 1, 2008
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Submitted on October 19, 2007
Revised on December 17, 2007
Accepted on January 17, 2008

Galectin-1 Is a Novel Structural Component and a Major Regulator of H-Ras Nanoclusters

Liron Belanis,*{dagger} Sarah J. Plowman,{dagger}{ddagger} Barak Rotblat,* John F. Hancock,{ddagger} and Yoel Kloog*

*Department of Neurobiochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel Aviv, Israel; {ddagger}Institute for Molecular Bioscience, University of Queensland, St Lucia, QLD 4072, Australia

Monitoring Editor: J. Silvio Gutkind

The organization of Ras proteins into nanoclusters on the inner plasma membrane is essential for Ras signal transduction, but the mechanisms that drive nanoclustering are unknown. Here we show that EGFR activation stimulates the formation of H-Ras.GTP- Galectin-1 (Gal-1) complexes on the plasma membrane that are then assembled into transient nanoclusters. Gal-1 is therefore an integral structural component of the H-Ras signaling nanocluster. Increasing Gal-1 levels increases the stability of H-Ras nanoclusters leading to enhanced effector recruitment and signal output. Elements in the H-Ras C-terminal hypervariable region and an activated G-domain are required for H-Ras-Gal-1 interaction. Palmitoylation is not required for H-Ras-Gal-1 complex formation, but is required to anchor H-Ras-Gal-1 complexes to the plasma membrane. Our data suggest a mechanism for H-Ras nanoclustering that involves a dual role for Gal-1 as a critical scaffolding protein and a molecular chaperone that contributes to H-Ras trafficking by returning depalmitoylated H-Ras to the Golgi complex for repalmitoylation.

{dagger}These authors contributed equally to this work.

Address correspondence to: John F. Hancock (j.hancock{at}imb.uq.edu.au) or Yoel Kloog (kloog{at}post.tau.ac.il)




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