A lipid bound actin meshwork organizes liquid phase separation in model membranes

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung

Beitragende

  • Alf Honigmann - , Max-Planck-Institut für biophysikalische Chemie (Karl-Friedrich-Bonhoeffer-Institut) (Autor:in)
  • Sina Sadeghi - , Georg-August-Universität Göttingen (Autor:in)
  • Jan Keller - , Max-Planck-Institut für biophysikalische Chemie (Karl-Friedrich-Bonhoeffer-Institut) (Autor:in)
  • Stefan W. Hell - , Max-Planck-Institut für biophysikalische Chemie (Karl-Friedrich-Bonhoeffer-Institut) (Autor:in)
  • Christian Eggeling - , Max-Planck-Institut für biophysikalische Chemie (Karl-Friedrich-Bonhoeffer-Institut), University of Oxford (Autor:in)
  • Richard Vink - , Georg-August-Universität Göttingen (Autor:in)

Abstract

The eukaryotic cell membrane is connected to a dense actin rich cortex. We present FCS and STED experiments showing that dense membrane bound actin networks have severe influence on lipid phase separation. A minimal actin cortex was bound to a supported lipid bilayer via biotinylated lipid streptavidin complexes (pinning sites). In general, actin binding to ternary membranes prevented macroscopic liquid-ordered and liquid-disordered domain formation, even at low temperature. Instead, depending on the type of pinning lipid, an actin correlated multi-domain pattern was observed. FCS measurements revealed hindered diffusion of lipids in the presence of an actin network. To explain our experimental findings, a new simulation model is proposed, in which the membrane composition, the membrane curvature, and the actin pinning sites are all coupled. Our results reveal a mechanism how cells may prevent macroscopic demixing of their membrane components, while at the same time regulate the local membrane composition.

Details

OriginalspracheEnglisch
Aufsatznummere01671
FachzeitschrifteLife
Jahrgang2014
Ausgabenummer3
PublikationsstatusVeröffentlicht - 18 März 2014
Peer-Review-StatusJa
Extern publiziertJa

Externe IDs

PubMed 24642407
ORCID /0000-0003-0475-3790/work/161889558