| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5671751 | Current Opinion in Microbiology | 2017 | 9 Pages |
â¢Functional membrane microdomains promote efficient oligomerization of protein partners.â¢They form by colocalization of specific lipids and scaffold proteins termed flotillins.â¢These domains are found in Gram-positive and -negative bacteria, and also archea.â¢Membrane microdomain integrity is important for associated oligomer activity.
Recent studies show that internal organization of bacterial cells is more complex than previously appreciated. A clear example of this is the assembly of the nanoscale membrane platforms termed functional membrane microdomains. The lipid composition of these regions differs from that of the surrounding membrane; these domains confine a set of proteins involved in specific cellular processes such as protease secretion and signal transduction. It is currently thought that functional membrane microdomains act as oligomerization platforms and promote efficient oligomerization of interacting protein partners in bacterial membranes. In this review, we highlight the most noteworthy achievements, challenges and controversies of this emerging research field over the past five years.
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