Higher-order assemblies of BAR domain proteins for shaping membranes

Microscopy
Shiro Suetsugu

Abstract

Most cellular organelles contain lipid bilayer membranes. The earliest characterization of cellular organelles was performed by electron microscopy observation of such membranes. However, the precise mechanisms for shaping the membrane in particular subcellular organelles is poorly understood. Classically, the overall cellular shape, i.e. the shape of the plasma membrane, was thought to be governed by the reorganization of cytoskeletal components such as actin and microtubules. The plasma membrane contains various submicron structures such as clathrin-coated pits, caveolae, filopodia and lamellipodia. These subcellular structures are either invaginations or protrusions and are associated with the cytoskeleton. Therefore, it could be hypothesized that there are membrane-binding proteins that cooperates with cytoskeleton in shaping of plasma membrane organelles. Proteins with the Bin-Amphiphysin-Rvs (BAR) domain connect a variety of membrane shapes to actin filaments. The BAR domains themselves bend the membranes by their rigidity and then mold the membranes into tubules through their assembly as spiral polymers, which are thought to be involved in the various submicron structures. Membrane tubulation by polymeric assembly of the...Continue Reading

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Citations

Mar 8, 2017·Scientific Reports·Yu SasakiKatsuhiko Asanuma
Jul 1, 2017·Molecular Biology of the Cell·Michael M LacyJulien Berro
Oct 27, 2017·The Journal of Cell Biology·Jean A SmithMark D Rose
Aug 2, 2021·Biochimica Et Biophysica Acta. General Subjects·Chandra Has, Sovan Lal Das
Jul 11, 2020·Langmuir : the ACS Journal of Surfaces and Colloids·Andrea AuerswaldAnnette Meister

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