Evidence map›Paper›PMID 21059949›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2).

David Schwefel, Chris Fröhlich, Jenny Eichhorst, Burkhard Wiesner, Joachim Behlke, L Aravind, Oliver Daumke

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Upregulated small GTPase immunity-associated proteins confer resistance toFrontiers in cellular and infection microbiology · 2025
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  16. [Subcellular localization of GTPase of immunity-associated protein 2].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

David SchwefelMax-Delbrück-Centrum für Molekulare Medizin, Kristallographie, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.
Chris Fröhlich
Jenny Eichhorst
Burkhard Wiesner
Joachim Behlke
L Aravind
Oliver Daumke
Max Delbrück Center · DELeibniz-Forschungsinstitut für Molekulare Pharmakologie · DEFreie Universität Berlin · DENational Center for Biotechnology Information · US

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

GTPases of immunity-associated proteins (GIMAPs) are a distinctive family of GTPases, which control apoptosis in lymphocytes and play a central role in lymphocyte maturation and lymphocyte-associated diseases. To explore their function and mechanism, we determined crystal structures of a representative member, GIMAP2, in different nucleotide-loading and oligomerization states. Nucleotide-free and GDP-bound GIMAP2 were monomeric and revealed a guanine nucleotide-binding domain of the TRAFAC (translation factor associated) class with a unique amphipathic helix α7 packing against switch II. In the absence of α7 and the presence of GTP, GIMAP2 oligomerized via two distinct interfaces in the crystal. GTP-induced stabilization of switch I mediates dimerization across the nucleotide-binding site, which also involves the GIMAP specificity motif and the nucleotide base. Structural rearrangements in switch II appear to induce the release of α7 allowing oligomerization to proceed via a second interface. The unique architecture of the linear oligomer was confirmed by mutagenesis. Furthermore, we showed a function for the GIMAP2 oligomer at the surface of lipid droplets. Although earlier studies indicated that GIMAPs are related to the septins, the current structure also revealed a strikingly similar nucleotide coordination and dimerization mode as in the dynamin GTPase. Based on this, we reexamined the relationships of the septin- and dynamin-like GTPases and demonstrate that these are likely to have emerged from a common membrane-associated dimerizing ancestor. This ancestral property appears to be critical for the role of GIMAPs as nucleotide-regulated scaffolds on intracellular membranes.

Indexed as

Models, MolecularPhylogenyProtein ConformationProtein Structure, TertiaryCalorimetryChromatography, High Pressure LiquidCrystallizationDimerizationGTP PhosphohydrolasesHumansHydrolysisJurkat CellsMembrane ProteinsMutagenesisNucleotidesUltracentrifugationGIMAP2 protein, humanGTP PhosphohydrolasesMembrane ProteinsNucleotides

Identifiers

PMID21059949
PMCPMC2996681
OpenAlexW2065853723

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.