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Effects of protein crowding on membrane systems
- Source :
- Biochimica et biophysica acta. 1858(10)
- Publication Year :
- 2015
-
Abstract
- Cellular membranes are typically decorated with a plethora of embedded and adsorbed macromolecules, e.g. proteins, that participate in numerous vital processes. With typical surface densities of 30,000 proteins per μm(2) cellular membranes are indeed crowded places that leave only few nanometers of private space for individual proteins. Here, we review recent advances in our understanding of protein crowding in membrane systems. We first give a brief overview on state-of-the-art approaches in experiment and simulation that are frequently used to study crowded membranes. After that, we review how crowding can affect diffusive transport of proteins and lipids in membrane systems. Next, we discuss lipid and protein sorting in crowded membrane systems, including effects like protein cluster formation, phase segregation, and lipid droplet formation. Subsequently, we highlight recent progress in uncovering crowding-induced conformational changes of membranes, e.g. membrane budding and vesicle formation. Finally, we give a short outlook on potential future developments in the field of crowded membrane systems. This article is part of a Special Issue entitled: Biosimulations edited by Ilpo Vattulainen and Tomasz Rog.
- Subjects :
- 0301 basic medicine
Membrane lipids
Biophysics
Molecular Conformation
Biology
010402 general chemistry
medicine.disease_cause
01 natural sciences
Biochemistry
Cell membrane
Diffusion
03 medical and health sciences
Membrane Lipids
Protein targeting
medicine
Membrane transport protein
Cell Membrane
Membrane Proteins
Cell Biology
Membrane budding
0104 chemical sciences
Cell biology
030104 developmental biology
medicine.anatomical_structure
Membrane
Membrane protein
biology.protein
Macromolecular crowding
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 1858
- Issue :
- 10
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....b7f2209d7f5c78373cd76aa4a7cd5c6a