Evidence map›Paper›PMID 20534488›Full record

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

Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of Early Endosomal Autoantigen 1 (EEA1).

Ashwini Mishra, Sudharshan Eathiraj, Silvia Corvera, David G Lambright

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 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

57 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
  2. Article
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  5. Article
  6. mBio · 2023
    Article
  7. AtypicalScience advances · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Poly(ADP-ribose) Polymerase 1 Mediates Rab5 Inactivation after DNA Damage.International journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. A New Hypothesis for Alzheimer's Disease: The Lipid Invasion Model.Journal of Alzheimer's disease reports · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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

4 authors at 3 institutions in 1 country.

Ashwini MishraDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Sudharshan Eathiraj
Silvia Corvera
David G Lambright
University of Massachusetts Chan Medical School · USHoward Hughes Medical Institute · USYale University · US

Funding

UMASS MEDICAL CENTER FOR AIDS RESEARCHP30AI042845 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LUZURIAGA, KATHERINE F · 1998 to 2012
$13.0M
STRUCTURAL BASIS OF G PROTEIN MEDIATED SIGNALINGR01GM056324 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LAMBRIGHT, DAVID G · 1998 to 2018
$6.2M
NIAID NIH HHS 5P30AI42845NIAID NIH HHS P30 AI042845NIGMS NIH HHS GM 056324NIGMS NIH HHS R01 GM056324
6 · The paper itself

Abstract

Regulation of endosomal trafficking by Rab GTPases depends on selective interactions with multivalent effectors, including EEA1 and Rabenosyn-5, which facilitate endosome tethering, sorting, and fusion. Both EEA1 and Rabenosyn-5 contain a distinctive N-terminal C(2)H(2) zinc finger that binds Rab5. How these C(2)H(2) zinc fingers recognize Rab GTPases remains unknown. Here, we report the crystal structure of Rab5A in complex with the EEA1 C(2)H(2) zinc finger. The binding interface involves all elements of the zinc finger as well as a short N-terminal extension but is restricted to the switch and interswitch regions of Rab5. High selectivity for Rab5 and, to a lesser extent Rab22, is observed in quantitative profiles of binding to Rab family GTPases. Although critical determinants are identified in both switch regions, Rab4-to-Rab5 conversion-of-specificity mutants reveal an essential requirement for additional substitutions in the proximal protein core that are predicted to indirectly influence recognition through affects on the structure and conformational stability of the switch regions.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAutoantigensCrystallography, X-RayEndosomesHumansIn Vitro TechniquesModels, MolecularMolecular Sequence DataMultiprotein ComplexesProtein Conformationrab4 GTP-Binding Proteinsrab5 GTP-Binding Proteinsrab GTP-Binding ProteinsRecombinant ProteinsSequence Homology, Amino AcidAutoantigensearly endosome antigen 1Multiprotein Complexesrab4 GTP-Binding Proteinsrab5 GTP-Binding Proteinsrab GTP-Binding ProteinsRBSN protein, humanRecombinant ProteinsVesicular Transport Proteins

Identifiers

PMID20534488
PMCPMC2890723
OpenAlexW1985778572

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.