Evidence map›Paper›PMID 27502489›Full record

ArticleThe Journal of cell biology2016

VPS35 binds farnesylated N-Ras in the cytosol to regulate N-Ras trafficking.

Mo Zhou, Heidi Wiener, Wenjuan Su, Yong Zhou, Caroline Liot, Ian Ahearn, John F Hancock, Mark R Philips

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

40 citing papers in PubMed, 59 citations in OpenAlex.

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  13. Fluorescent Biosensor for Measuring Ras Activity in Living Cells.Journal of the American Chemical Society · 2022
    Article
  14. Article
  15. Post-translational modification of RAS proteins.Current opinion in structural biology · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Depletion ofGenes & diseases · 2021
    Article
  20. Article
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 2 institutions in 1 country.

Mo ZhouPerlmutter Cancer Center, New York University School of Medicine, New York, NY 10016.ORCID 0000-0002-0416-9132
Heidi WienerPerlmutter Cancer Center, New York University School of Medicine, New York, NY 10016.
Wenjuan SuPerlmutter Cancer Center, New York University School of Medicine, New York, NY 10016.
Yong ZhouDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, Houston, TX 77030.ORCID 0000-0002-0214-8151
Caroline LiotPerlmutter Cancer Center, New York University School of Medicine, New York, NY 10016.
Ian AhearnPerlmutter Cancer Center, New York University School of Medicine, New York, NY 10016.ORCID 0000-0002-2275-137X
John F HancockDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, Houston, TX 77030.
Mark R PhilipsPerlmutter Cancer Center, New York University School of Medicine, New York, NY 10016 philim01@nyumc.org.ORCID 0000-0002-1179-8156
New York University · USThe University of Texas Health Science Center at Houston · US

Funding

Regulation of K-Ras by a Farnesyl-electrostatic SwitchR01CA116034 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2005 to 2017
$3.4M
Membrane Targeting of GTPasesR01GM055279 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 1997 to 2010
$3.2M
Isoprenylcysteine Carboxyl Methyltransferase (ICMT) as a Target in NRAS Driven Melanoma - Resubmission - 1R01CA163489 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2012 to 2020
$2.8M
NCI NIH HHS R01 CA116034NCI NIH HHS R01 CA163489NIGMS NIH HHS R01 GM055279
6 · The paper itself

Abstract

Ras guanosine triphosphatases (GTPases) regulate signaling pathways only when associated with cellular membranes through their C-terminal prenylated regions. Ras proteins move between membrane compartments in part via diffusion-limited, fluid phase transfer through the cytosol, suggesting that chaperones sequester the polyisoprene lipid from the aqueous environment. In this study, we analyze the nature of the pool of endogenous Ras proteins found in the cytosol. The majority of the pool consists of farnesylated, but not palmitoylated, N-Ras that is associated with a high molecular weight (HMW) complex. Affinity purification and mass spectrographic identification revealed that among the proteins found in the HMW fraction is VPS35, a latent cytosolic component of the retromer coat. VPS35 bound to N-Ras in a farnesyl-dependent, but neither palmitoyl- nor guanosine triphosphate (GTP)-dependent, fashion. Silencing VPS35 increased N-Ras's association with cytoplasmic vesicles, diminished GTP loading of Ras, and inhibited mitogen-activated protein kinase signaling and growth of N-Ras-dependent melanoma cells.

Indexed as

Protein PrenylationAnimalsCell Line, TumorCytosolDogsGene SilencingGreen Fluorescent ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHEK293 CellsHumansJurkat CellsLipoylationMadin Darby Canine Kidney CellsMelanomaMembrane ProteinsGreen Fluorescent ProteinsGTP PhosphohydrolasesGuanosine TriphosphateMembrane ProteinsMutant ProteinsNRAS protein, humanVesicular Transport ProteinsVPS35 protein, human

Identifiers

PMID27502489
PMCPMC4987297
OpenAlexW2476034752

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.