Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts

doi:10.1083/jcb.200308142

Published online 17 November 2003. doi:10.1083/jcb.200308142

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© The Rockefeller University Press, 0021-9525/2003/11/879 $8.00
The Journal of Cell Biology, Volume 163, Number 4, 879-888

Article

Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts

Dmitry E. Shvartsman¹, Mariana Kotler¹, Renee D. Tall², Michael G. Roth² and Yoav I. Henis¹

¹ Department of Neurobiochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
² Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235

Address correspondence to Yoav I. Henis, Dept. of Neurobiochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. Tel.: (972)-3-640-9053. Fax: (972)-3-640-7643. email: henis{at}post.tau.ac.il

Lipid rafts play important roles in cellular functions throughconcentrating or sequestering membrane proteins. This requiresproteins to differ in the stability of their interactions withlipid rafts. However, knowledge of the dynamics of membraneprotein–raft interactions is lacking. We employed FRAPto measure in live cells the lateral diffusion of influenzahemagglutinin (HA) proteins that differ in raft association.This approach can detect weak interactions with rafts not detectableby biochemical methods. Wild-type (wt) HA and glycosylphosphatidylinositol(GPI)-anchored HA (BHA-PI) diffused slower than a nonraft HAmutant, but became equal to the latter after cholesterol depletion.When antigenically distinct BHA-PI and wt HA were coexpressed,aggregation of BHA-PI into immobile patches reduced wt HA diffusionrate, suggesting transient interactions with BHA-PI raft patches.Conversely, patching wt HA reduced the mobile fraction of BHA-PI,indicating stable interactions with wt HA patches. Thus, theanchoring mode determines protein–raft interaction dynamics.GPI-anchored and transmembrane proteins can share the same rafts,and different proteins can interact stably or transiently withthe same raft domains.

Key Words: influenza hemagglutinin; rafts; fluorescence; lateral diffusion; photobleaching

Abbreviations used in this paper: DRM, detergent-resistant membrane;GPI, glycosylphosphatidylinositol; TM, transmembrane; wt, wildtype.

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