PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 9635431

Dynamin undergoes a GTP-dependent conformational change causing vesiculation.

S M Sweitzer·J E Hinshaw
View original source ↗Export metadata ↓

Abstract

The dynamin family of GTPases is essential for receptor-mediated endocytosis and synaptic vesicle recycling, and it has recently been shown to play a role in vesicle formation from the trans-Golgi network. Dynamin is believed to assemble around the necks of clathrin-coated pits and assist in pinching vesicles from the plasma membrane. This role would make dynamin unique among GTPases in its ability to act as a mechanochemical enzyme. Data presented here demonstrate that purified recombinant dynamin binds to a lipid bilayer in a regular pattern to form helical tubes that constrict and vesiculate upon GTP addition. This suggests that dynamin alone is sufficient for the formation of constricted necks of coated pits and supports the hypothesis that dynamin is the force-generating molecule responsible for membrane fission.

Explore related subjects

DynaminsGTP PhosphohydrolasesGuanosine TriphosphateHydrolysisLightLipid BilayersLiposomesPhosphatidylserinesPhosphorylationProlineProtein BindingProtein ConformationProtein Kinase CRecombinant Fusion ProteinsScattering, RadiationSubtilisinsJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

S M Sweitzer, J E Hinshaw. 1998-06-12. Dynamin undergoes a GTP-dependent conformational change causing vesiculation.. https://doi.org/10.1016/s0092-8674(00)81207-6

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2006

Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1.

Mitochondrial outer- and inner-membrane fusion events are coupled in vivo but separable and mechanistically distinct in vitro, indicating that separate fusion machines exist in each membrane. Outer-membrane fusion requires trans interactions of the dynamin-related GTPase Fzo1, GTP hydrolysis, and an intact inner-membrane proton gradient. Inner-membrane fusion also requires GTP hydrolysis but distinctly requires an inner-membrane electrical potential. The protein machinery responsible for inner-membrane fusion is unknown. Here, we show that the conserved intermembrane-space dynamin-related GTPase Mgm1 is required to tether and fuse mitochondrial inner membranes. We observe an additional role of Mgm1 in inner-membrane dynamics, specifically in the maintenance of crista structures. We present evidence that trans Mgm1 interactions on opposing inner membranes function similarly to tether and fuse inner membranes as well as maintain crista structures and propose a model for how the mitochondrial dynamins function to facilitate fusion.

Dynamins↗
PubMed2006

Dissecting mitochondrial fusion.

Because mitochondria have outer and inner membranes, the fusion of two mitochondria requires the coordinated fusion of four lipid bilayers. Fusion of the outer membranes requires mitofusins. A new study published in Cell (Meeusen et al., 2006) shows that inner membrane fusion requires the dynamin-related protein Mgm1/OPA1.

Dynamins↗