Abstract:
:Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis to membrane deformation, which eventually leads to fusion or fission of the lipid bilayer. Mutations in eukaryotic dynamin-like proteins (DLPs) are associated with various diseases underscoring the importance to fully understand the biochemistry of these proteins. In recent years, a wealth of structural and biochemical data have been published that allow a detailed analysis of how dynamins or DLPs modulate biological membranes. However, less is known about the function of bacterial DLPs, although structural data exist. This review summarizes current knowledge about bacterial dynamins and discusses structural and functional properties in comparison to their eukaryotic counterparts.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Bramkamp Mdoi
10.1515/hsz-2012-0185subject
Has Abstractpub_date
2012-11-01 00:00:00pages
1203-14issue
11eissn
1431-6730issn
1437-4315pii
/j/bchm.2012.393.issue-11/hsz-2012-0185/hsz-2012-0journal_volume
393pub_type
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