The interactions of peripheral membrane proteins with biological membranes

A. M. Whited, A. Johs

Research output: Contribution to journalArticlepeer-review

74 Scopus citations

Abstract

The interactions of peripheral proteins with membrane surfaces are critical to many biological processes, including signaling, recognition, membrane trafficking, cell division and cell structure. On a molecular level, peripheral membrane proteins can modulate lipid composition, membrane dynamics and protein-protein interactions. Biochemical and biophysical studies have shown that these interactions are in fact highly complex, dominated by several different types of interactions, and have an interdependent effect on both the protein and membrane. Here we examine three major mechanisms underlying the interactions between peripheral membrane proteins and membranes: electrostatic interactions, hydrophobic interactions, and fatty acid modification of proteins. While experimental approaches continue to provide critical insights into specific interaction mechanisms, emerging bioinformatics resources and tools contribute to a systems-level picture of protein-lipid interactions. Through these recent advances, we begin to understand the pivotal role of protein-lipid interactions underlying complex biological functions at membrane interfaces.

Original languageEnglish
Pages (from-to)51-59
Number of pages9
JournalChemistry and Physics of Lipids
Volume192
DOIs
StatePublished - Nov 1 2015

Funding

This research was supported by the Laboratory Directed Research and Development Program of the Oak Ridge National Laboratory (ORNL) . ORNL is managed by UT-Battelle, LLC under contract no. DE-AC05-00OR22725 with the US Department of Energy. The United States Government retains and the publisher, by accepting the article for publication, acknowledges that the United States Government retains a non-exclusive, paid-up, irrevocable, world-wide license to publish or reproduce the published form of this manuscript, or allow others to do so, for United States Government purposes. The Department of Energy will provide public access to these results of federally sponsored research in accordance with the DOE Public Access Plan ( http://energy.gov/downloads/doe-public-access-plan ).

Keywords

  • Electrostatic interactions
  • Fatty acid modification
  • Hydrophobic interactions
  • Lipids
  • Membrane
  • Peripheral membrane proteins

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