title: Membrane-mediated interactions--a physico-chemical basis for protein sorting.
abstract: Sorting of membrane proteins in eukaryotic cells is a complex yet vital task that involves several 10,000 molecular players. Sorting takes place not only along the early secretory pathway, i.e., between the endoplasmic reticulum and the Golgi apparatus, but also between other organelles, including exchange with the cell's plasma membrane. Traditionally, specific binary interactions between proteins have been made responsible for most of the protein sorting. A more active role of lipids, however, became visible in recent years. Not only do lipids in complex membranes show domain formation that may support/suppress sorting events, but also collective, membrane-mediated interactions have emerged as a robust physico-chemical mechanism to drive protein sorting. Here, we will review recent insights into these aspects.
authors.affiliation: Experimental Physics I, University of Bayreuth, Bayreuth, Germany.
authors.forename: Mária
authors.initials: M
authors.lastname: Hanulová
authors.forename: Matthias
authors.initials: M
authors.lastname: Weiss
mesh_terms: D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D021381:Protein Transport; D055571:Secretory Pathway
chemical_list: D008565:Membrane Proteins