title: Cytoskeletal Components Define Protein Location to Membrane Microdomains.
abstract: The plasma membrane is an important compartment that undergoes dynamic changes in composition upon external or internal stimuli. The dynamic subcompartmentation of proteins in ordered low-density (DRM) and disordered high-density (DSM) membrane phases is hypothesized to require interactions with cytoskeletal components. Here, we systematically analyzed the effects of actin or tubulin disruption on the distribution of proteins between membrane density phases. We used a proteomic screen to identify candidate proteins with altered submembrane location, followed by biochemical or cell biological characterization in Arabidopsis thaliana. We found that several proteins, such as plasma membrane ATPases, receptor kinases, or remorins resulted in a differential distribution between membrane density phases upon cytoskeletal disruption. Moreover, in most cases, contrasting effects were observed: Disruption of actin filaments largely led to a redistribution of proteins from DRM to DSM membrane fractions while disruption of tubulins resulted in general depletion of proteins from the membranes. We conclude that actin filaments are necessary for dynamic movement of proteins between different membrane phases and that microtubules are not necessarily important for formation of microdomains as such, but rather they may control the protein amount present in the membrane phases.
authors.affiliation: From the ‡Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam, Germany;
authors.forename: Witold G
authors.initials: WG
authors.lastname: Szymanski
authors.affiliation: §Max-Delbrück Center of Molecular Medicine, Robert-Rössle-Straβe 10, 13092 Berlin, Germany;
authors.forename: Henrik
authors.initials: H
authors.lastname: Zauber
authors.affiliation: From the ‡Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam, Germany;
authors.forename: Alexander
authors.initials: A
authors.lastname: Erban
authors.affiliation: From the ‡Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam, Germany;
authors.forename: Michal
authors.initials: M
authors.lastname: Gorka
authors.affiliation: From the ‡Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam, Germany;
authors.forename: Xu Na
authors.initials: XN
authors.lastname: Wu
authors.affiliation: ¶University of Hohenheim, Department of Plant Systems Biology, 70593 Stuttgart, Germany wschulze@uni-hohenheim.de.
authors.forename: Waltraud X
authors.initials: WX
authors.lastname: Schulze
mesh_terms: D000199:Actins / Q000378:metabolism*; D017360:Arabidopsis / Q000166:cytology* / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D018929:Cell Culture Techniques; D002462:Cell Membrane / Q000378:metabolism; D040901:Proteomics / Q000379:methods; D014404:Tubulin / Q000378:metabolism*
chemical_list: D000199:Actins; D029681:Arabidopsis Proteins; D014404:Tubulin