2015
DOI: 10.1038/nature14880
|View full text |Cite
|
Sign up to set email alerts
|

Crystal structure of the dynamin tetramer

Abstract: The mechano-chemical protein dynamin is the prototype of the dynamin superfamily of large GTPases, which shape and remodel membranes in diverse cellular processes 1 .Dynamin forms predominantly tetramers in the cytosol, which oligomerize at the neck of clathrin-coated vesicles to mediate constriction and subsequent scission of the membrane 1 . Previous studies have described the architecture of dynamin dimers 2,3 , but the molecular determinants for dynamin assembly and its regulation have remained unclear. He… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1

Citation Types

10
164
0
1

Year Published

2016
2016
2022
2022

Publication Types

Select...
8

Relationship

2
6

Authors

Journals

citations
Cited by 122 publications
(175 citation statements)
references
References 51 publications
10
164
0
1
Order By: Relevance
“…S8). In the autoinhibited dynamin tetramer, an intramolecular contact of the pleckstrin homology (PH) domain with the oligomerization surface of the stalk prevents the assembly in the cytosol (25), whereas an autoinhibitory contact of the C-terminal EH domain with the GTPase domains takes over this function in EHDs. Such intramolecular inhibitory contacts are also observed in other peripheral or integral membrane proteins, such as BAR-domain containing proteins (26,27), SNAREs (28), ESCRT-III (29), or the WASP protein (30) (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…S8). In the autoinhibited dynamin tetramer, an intramolecular contact of the pleckstrin homology (PH) domain with the oligomerization surface of the stalk prevents the assembly in the cytosol (25), whereas an autoinhibitory contact of the C-terminal EH domain with the GTPase domains takes over this function in EHDs. Such intramolecular inhibitory contacts are also observed in other peripheral or integral membrane proteins, such as BAR-domain containing proteins (26,27), SNAREs (28), ESCRT-III (29), or the WASP protein (30) (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…The GTPase domain is connected to the stalk via a flexible hinge called a bundle signaling element (BSE) (4,5). The crystal structures also provided evidence on how molecular interactions between dimers lead to the formation of a helical polymer (1)(2)(3). In particular, in the tetrameric form (3), GTPase domains from two contiguous dynamin dimers are closely apposed.…”
mentioning
confidence: 94%
“…Dynamin has a relatively low affinity for both GTP and GDP (38), therefore release of GDP does not require presence of designated GEFs, nor is dynamin: GDP conformation stabilized by the presence of GDIs. A striking feature of dynamin assembly into higher order structures is the multitude of interactions in all four molecules (36). Structural data suggest that these contacts are not necessarily static, but characterized by a dynamic equilibrium of different binding conformations.…”
Section: Actin Cytoskeleton Dynamics As a Pharmacological Target In Kmentioning
confidence: 99%
“…The molecular mechanism by which dynamin releases gelsolin from the barbed ends is at present unknown, but fluorescence lifetime imaging microscopy suggests that it requires GTP binding and a major conformational change within dynamin tetramers (40). The conformational change might be similar to the one suggested for dynamin assembly on the lipids (36,40).…”
Section: Actin Cytoskeleton Dynamics As a Pharmacological Target In Kmentioning
confidence: 99%
See 1 more Smart Citation