Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein

Ana West, Benjamin E. Brummel, Anthony R. Braun, Elizabeth Rhoades, Jonathan N. Sachs

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

We review experimental and simulation approaches that have been used to determine curvature generation and remodeling of lipid bilayers by membrane-bending proteins. Particular emphasis is placed on the complementary approaches used to study α-Synuclein (αSyn), a major protein involved in Parkinson's disease (PD). Recent cellular and biophysical experiments have shown that the protein 1) deforms the native structure of mitochondrial and model membranes; and 2) inhibits vesicular fusion. Today's advanced experimental and computational technology has made it possible to quantify these protein-induced changes in membrane shape and material properties. Collectively, experiments, theory and multi-scale simulation techniques have established the key physical determinants of membrane remodeling and rigidity: protein binding energy, protein partition depth, protein density, and membrane tension. Despite the exciting and significant progress made in recent years in these areas, challenges remain in connecting biophysical insights to the cellular processes that lead to disease. This article is part of a Special Issue entitled: Membrane Proteins edited by J.C. Gumbart and Sergei Noskov.

Original languageEnglish (US)
Pages (from-to)1594-1609
Number of pages16
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1858
Issue number7
DOIs
StatePublished - Jul 1 2016

Bibliographical note

Funding Information:
This work was supported by the National Institutes of Health ( R01 NS084998 to J.N.S.).

Keywords

  • Bilayer rigidity
  • Coarse-grained molecular dynamics (CGMD)
  • Membrane curvature
  • Parkinson's disease
  • Synaptic vesicles
  • Tubulation
  • α-Synuclein

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