Evidence map›Paper›PMID 18458061›Full record

ArticleMolecular and cellular biology2008

Electrostatic interactions positively regulate K-Ras nanocluster formation and function.

Sarah J Plowman, Nicholas Ariotti, Andrew Goodall, Robert G Parton, John F Hancock

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

64 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. A structural model of a Ras-Raf signalosome.Nature structural & molecular biology · 2021
    Article
  9. Article
  10. Article
  11. Unveiling the Dynamics of KRAS4b on Lipid Model Membranes.The Journal of membrane biology · 2021
    Article
  12. Review
  13. Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Ras and the Plasma Membrane: A Complicated Relationship.Cold Spring Harbor perspectives in medicine · 2018
    Review
  18. Article
  19. Review
  20. Article

4 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

5 authors at 1 institution in 1 country.

Sarah J PlowmanInstitute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.
Nicholas Ariotti
Andrew Goodall
Robert G Parton
John F Hancock
University of Queensland · AU

Funding

Structure and Function of Plasma membrane NanodomainsR01GM066717 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI HANCOCK, JOHN F · 2003 to 2012
$2.4M
NIGMS NIH HHS GM-066717NIGMS NIH HHS R01 GM066717
6 · The paper itself

Abstract

The organization of Ras proteins into plasma membrane nanoclusters is essential for high-fidelity signal transmission, but whether the nanoscale environments of different Ras nanoclusters regulate effector interactions is unknown. We show using high-resolution spatial mapping that Raf-1 is recruited to and retained in K-Ras-GTP nanoclusters. In contrast, Raf-1 recruited to the plasma membrane by H-Ras is not retained in H-Ras-GTP nanoclusters. Similarly, upon epidermal growth factor receptor activation, Raf-1 is preferentially recruited to K-Ras-GTP and not H-Ras-GTP nanoclusters. The formation of K-Ras-GTP nanoclusters is inhibited by phosphorylation of S181 in the C-terminal polybasic domain or enhanced by blocking S181 phosphorylation, with a concomitant reduction or increase in Raf-1 plasma membrane recruitment, respectively. Phosphorylation of S181 does not, however, regulate in vivo interactions with the nanocluster scaffold galectin-3 (Gal3), indicating separate roles for the polybasic domain and Gal3 in driving K-Ras nanocluster formation. Together, these data illustrate that Ras nanocluster composition regulates effector recruitment and highlight the importance of lipid/protein nanoscale environments to the activation of signaling cascades.

Indexed as

AnimalsCell LineCell MembraneCricetinaeEpidermal Growth FactorGuanosine TriphosphateMAP Kinase Signaling SystemPC12 CellsProtein IsoformsProtein Structure, TertiaryProto-Oncogene Proteins c-rafras ProteinsRatsStatic ElectricityTranscription FactorsEpidermal Growth FactorGuanosine TriphosphateProtein IsoformsProto-Oncogene Proteins c-rafras ProteinsTranscription Factors

Identifiers

PMID18458061
PMCPMC2447143
OpenAlexW2152821435

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.