Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2011 Feb 8;108(6):2175-6.
doi: 10.1073/pnas.1019194108. Epub 2011 Jan 28.

Structural insights into membrane fusion at the endoplasmic reticulum

Oliver Daumke  1 , Gerrit J K Praefcke
Affiliations
Comment

Structural insights into membrane fusion at the endoplasmic reticulum

Oliver Daumke et al. Proc Natl Acad Sci U S A. .
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Model for membrane fusion catalyzed by atlastins (Left) and BDLP (Right). Two atlastin molecules located at opposing membranes assemble through their G domains in a GTP-dependent fashion, with a dimer arrangement as seen in crystal form 2. The second cytosolic domain of atlastin is indicated as a dashed line. Reticulons, DP1 family proteins, and spastin facilitate the creation of membrane curvature. After GTP hydrolysis-dependent membrane fusion and establishment of a three-way junction, the two atlastin molecules might adopt a conformation as seen in crystal form 1. In BDLP, the MD contributes to the neck, trunk, and tip domains. BDLP molecules in the GTP-bound form oligomerize in cis, thus inducing membrane tubulation and extreme membrane curvature (indicated by the red stars), especially at or close to the tip of the membrane tubule (13). After GTP hydrolysis, the BDLP coat collapses allowing membrane fusion. Interestingly, the relative arrangement of G domain and MD in atlastin-1 crystal form 1 resembles the open oligomerized conformation of BDLP, whereas crystal form 2 of atlastin-1 has a similar relative domain arrangement as the closed state of BDLP.
See this image and copyright information in PMC

Comment on

References

    1. Orso G, et al. Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature. 2009;460:978–983. - PubMed
    1. Hu J, et al. A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell. 2009;138:549–561. - PMC - PubMed
    1. Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell. 2006;124:573–586. - PubMed
    1. Byrnes LJ, Sondermann H. Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A. Proc Natl Acad Sci USA. 2011;108:2216–2221. - PMC - PubMed
    1. Praefcke GJ, McMahon HT. The dynamin superfamily: Universal membrane tubulation and fission molecules? Nat Rev Mol Cell Biol. 2004;5:133–147. - PubMed

MeSH terms

LinkOut - more resources