Evidence map›Paper›PMID 18715992›Full record

ArticleProtein science : a publication of the Protein Society2008

Structure of a signal transduction regulator, RACK1, from Arabidopsis thaliana.

Hemayet Ullah, Erica Louise Scappini, Andrea Florence Moon, Latanya Veronica Williams, David Lee Armstrong, Lars Christian Pedersen

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
12.6field-weighted citation impact, top 1% 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

74 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. RACK1A positively regulates opening of the apical hook inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 1 country.

Hemayet UllahDepartment of Biology, Howard University, Washington, DC 20059, USA.
Erica Louise Scappini
Andrea Florence Moon
Latanya Veronica Williams
David Lee Armstrong
Lars Christian Pedersen
Howard University · USNational Institute of Environmental Health Sciences · USNational Institutes of Health · US

Funding

Crystallographic studies of macromolecular structuresZIAES102645 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI PEDERSEN, LARS · 2009 to 2017
$9.4M
Ion Channel Regulation By Signal Transduction PathwaysZIAES080043 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI ARMSTRONG, DAVID · 2009 to 2014
$6.7M
ION CHANNEL REGULATION BY SIGNAL TRANSDUCTION PATHWAYSZ01ES080043 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI ARMSTRONG, DAVID L · 1988 to 2008
$3.0M
Intramural NIH HHS Z01 ES080043
6 · The paper itself

Abstract

The receptor for activated C-kinase 1 (RACK1) is a highly conserved WD40 repeat scaffold protein found in a wide range of eukaryotic species from Chlamydymonas to plants and humans. In tissues of higher mammals, RACK1 is ubiquitously expressed and has been implicated in diverse signaling pathways involving neuropathology, cellular stress, protein translation, and developmental processes. RACK1 has established itself as a scaffold protein through physical interaction with a myriad of signaling proteins ranging from kinases, phosphatases, ion channels, membrane receptors, G proteins, IP3 receptor, and with widely conserved structural proteins associated with the ribosome. In the plant Arabidopsis thaliana, RACK1A is implicated in diverse developmental and environmental stress pathways. Despite the functional conservation of RACK1-mediated protein-protein interaction-regulated signaling modes, the structural basis of such interactions is largely unknown. Here we present the first crystal structure of a RACK1 protein, RACK1 isoform A from Arabidopsis thaliana, at 2.4 A resolution, as a C-terminal fusion of the maltose binding protein. The structure implicates highly conserved surface residues that could play critical roles in protein-protein interactions and reveals the surface location of proposed post-transcriptionally modified residues. The availability of this structure provides a structural basis for dissecting RACK1-mediated cellular signaling mechanisms in both plants and animals.

Indexed as

Amino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsCarrier ProteinsCloning, MolecularCrystallizationCrystallography, X-RayHumansMaltose-Binding ProteinsMolecular Sequence DataProtein Structure, TertiaryReceptors, Cell SurfaceReceptors for Activated C KinaseRecombinant Fusion ProteinsSequence AlignmentArabidopsis ProteinsCarrier ProteinsMaltose-Binding ProteinsRACK1 protein, ArabidopsisReceptors, Cell SurfaceReceptors for Activated C KinaseRecombinant Fusion Proteins

Identifiers

PMID18715992
PMCPMC2548356
OpenAlexW2140216844

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.