Evidence map›Paper›PMID 25713064›Full record

ArticleThe Journal of biological chemistry2015

Mechanisms of membrane binding of small GTPase K-Ras4B farnesylated hypervariable region.

Hyunbum Jang, Sherwin J Abraham, Tanmay S Chavan, Ben Hitchinson, Lyuba Khavrutskii, Nadya I Tarasova, Ruth Nussinov, Vadim Gaponenko

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 112 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Differential functions of the KRAS splice variants.Biochemical Society transactions · 2023
    Review
  10. Review
  11. Article
  12. The mechanism of activation of MEK1 by B-Raf and KSR1.Cellular and molecular life sciences : CMLS · 2022
    Article
  13. Article
  14. The role of KRAS splice variants in cancer biology.Frontiers in cell and developmental biology · 2022
    Review
  15. Post-translational modification of RAS proteins.Current opinion in structural biology · 2021
    Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

15 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

8 authors at 4 institutions in 2 countries.

Hyunbum JangFrom the Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research and Cancer and Inflammation Program, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702.
Sherwin J AbrahamDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, California 94305, Departments of Biochemistry and Molecular Genetics and.
Tanmay S ChavanDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, California 94305, Medicinal Chemistry, University of Illinois, Chicago, Illinois 60607, and.
Ben HitchinsonDepartments of Biochemistry and Molecular Genetics and.
Lyuba KhavrutskiiFrom the Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research and Cancer and Inflammation Program, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702.
Nadya I TarasovaCancer and Inflammation Program, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702, Nadya.Tarasova@nih.gov.
Ruth NussinovFrom the Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research and Cancer and Inflammation Program, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702, Department of Human Molecular Genetics and Biochemistry, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel NussinoR@helix.nih.gov.
Vadim GaponenkoDepartments of Biochemistry and Molecular Genetics and Medicinal Chemistry, University of Illinois, Chicago, Illinois 60607, and vadimg@uic.edu.
National Institutes of Health · USStanford University · USUniversity of Illinois Chicago · USFrederick National Laboratory for Cancer Research · US

Funding

Protein Structure, Stability, and Amyloid FormationZIABC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$11.8M
Biomolecular Recognition and Binding MechanismsZIABC010441 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$9.4M
Inhibitors of protein-protein interactionsZIABC011306 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI TARASOVA, NADYA · 2010 to 2025
$7.3M
Design of Therapeutic Peptide-Based NanoparticlesR01CA135341 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GAPONENKO, VADIM V · 2010 to 2014
$1.5M
CCR NIH HHS HHSN261200800001CIntramural NIH HHSNCI NIH HHS HHSN261200800001ENCI NIH HHS R01 CA135341
6 · The paper itself

Abstract

K-Ras4B belongs to a family of small GTPases that regulates cell growth, differentiation and survival. K-ras is frequently mutated in cancer. K-Ras4B association with the plasma membrane through its farnesylated and positively charged C-terminal hypervariable region (HVR) is critical to its oncogenic function. However, the structural mechanisms of membrane association are not fully understood. Here, using confocal microscopy, surface plasmon resonance, and molecular dynamics simulations, we observed that K-Ras4B can be distributed in rigid and loosely packed membrane domains. Its membrane binding domain interaction with phospholipids is driven by membrane fluidity. The farnesyl group spontaneously inserts into the disordered lipid microdomains, whereas the rigid microdomains restrict the farnesyl group penetration. We speculate that the resulting farnesyl protrusion toward the cell interior allows oligomerization of the K-Ras4B membrane binding domain in rigid microdomains. Unlike other Ras isoforms, K-Ras4B HVR contains a single farnesyl modification and positively charged polylysine sequence. The high positive charge not only modulates specific HVR binding to anionic phospholipids but farnesyl membrane orientation. Phosphorylation of Ser-181 prohibits spontaneous farnesyl membrane insertion. The mechanism illuminates the roles of HVR modifications in K-Ras4B targeting microdomains of the plasma membrane and suggests an additional function for HVR in regulation of Ras signaling.

Indexed as

Amino Acid SequenceAnimalsCell LineCell MembraneGTP PhosphohydrolasesHumansLipid BilayersMembrane FluidityMembrane MicrodomainsMicroscopy, ConfocalModels, ChemicalMolecular Dynamics SimulationMolecular Sequence DataPeptidesPhospholipidsPhosphorylationGTP PhosphohydrolasesKRAS protein, humanLipid BilayersPeptidesPhospholipidsProto-Oncogene Proteins p21(ras)SerineCooperativityHVRMembrane MicrodomainsPhospholipidPhosphorylationPost-translational Modification (PTM)Protein Isoprenylation

Identifiers

PMID25713064
PMCPMC4392252
OpenAlexW2006467878

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.