Evidence map›Paper›PMID 19158273›Full record

ArticleMolecular and cellular biology2009

Topology of mammalian isoprenylcysteine carboxyl methyltransferase determined in live cells with a fluorescent probe.

Latasha P Wright, Helen Court, Adam Mor, Ian M Ahearn, Patrick J Casey, Mark R Philips

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Posttranslational Modifications of RAS Proteins.Cold Spring Harbor perspectives in medicine · 2018
    Review
  6. Article
  7. Article
  8. Article
  9. Protein prenylation: unique fats make their mark on biology.Nature reviews. Molecular cell biology · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Regulating the regulator: post-translational modification of RAS.Nature reviews. Molecular cell biology · 2011
    Review
  16. Article
  17. Article
  18. 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

6 authors at 2 institutions in 1 country.

Latasha P WrightNYU Cancer Institute and Departments of Medicine, Cell Biology, and Pharmacology, NYU School of Medicine, New York, New York 10016, USA.
Helen Court
Adam Mor
Ian M Ahearn
Patrick J Casey
Mark R Philips
New York University · USDuke Medical Center · US

Funding

Membrane Targeting of GTPasesR01GM055279 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 1997 to 2010
$3.2M
Structure/Function Analysis of IcmtR01CA118495 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2006 to 2010
$1.5M
NCI NIH HHS CA118495NCI NIH HHS R01 CA118495NIGMS NIH HHS GM55279NIGMS NIH HHS R01 GM055279
6 · The paper itself

Abstract

Isoprenylcysteine carboxyl methyltransferase (Icmt) is a highly conserved enzyme that methyl esterifies the alpha carboxyl group of prenylated proteins including Ras and related GTPases. Methyl esterification neutralizes the negative charge of the prenylcysteine and thereby increases membrane affinity. Icmt is an integral membrane protein restricted to the endoplasmic reticulum (ER). The Saccharomyces cerevisiae ortholog, Ste14p, traverses the ER membrane six times. We used a novel fluorescent reporter to map the topology of human Icmt in living cells. Our results indicate that Icmt traverses the ER membrane eight times, with both N and C termini disposed toward the cytosol and with a helix-turn-helix structure comprising transmembrane (TM) segments 7 and 8. Several conserved amino acids that map to cytoplasmic portions of the enzyme are critical for full enzymatic activity. Mammalian Icmt has an N-terminal extension consisting of two TM segments not found in Ste14p and therefore likely to be regulatory. Icmt is a target for anticancer drug discovery, and these data may facilitate efforts to develop small-molecule inhibitors.

Indexed as

Amino Acid SubstitutionAnimalsAsparagineCell SurvivalChlorocebus aethiopsConserved SequenceCOS CellsCytosolEndoplasmic ReticulumFluorescent DyesGlycosylationHumansKineticsMutant ProteinsProlineProtein MethyltransferasesAsparagineFluorescent DyesMutant ProteinsProlineProtein Methyltransferasesprotein-S-isoprenylcysteine O-methyltransferase

Identifiers

PMID19158273
PMCPMC2655619
OpenAlexW2151023900

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.