Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 20, Issue 6, Pages 791-798Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2010.09.011
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Funding
- BBSRC [BB/F006284/1] Funding Source: UKRI
- MRC [MC_U105184326] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F006284/1] Funding Source: researchfish
- Medical Research Council [MC_U105184326] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/F006284/1] Funding Source: Medline
- Medical Research Council [MC_U105184326] Funding Source: Medline
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Dynamins form a family of eukaryotic and prokaryotic proteins involved in membrane fission, fusion and restructuring. They have complex mechanisms of self-assembly, which are coupled to the tubulation and destabilization of lipid bilayers. Recent structural data has revolutionized our understanding and is now yielding detailed insights into dynamin structure, from monomer through to polymer. Traditional division of the dynamin subunit into GTPase domain, middle domain and GTPase effector domain based on sequence alignments and biochemistry is not supported by recent structural data. A unified model of dynamin architecture is presented here, based on observation that the basic dynamin fold is conserved across evolutionary kingdoms.
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