Evidence map›Paper›PMID 10893259›Full record

ArticleThe Journal of cell biology2000

Molecular basis for Rab prenylation.

C Alory, W E Balch

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.1field-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

14 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  9. Mutation of the zebrafish choroideremia gene encoding Rab escort protein 1 devastates hair cells.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
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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

2 authors at 1 institution in 1 country.

C AloryDepartments of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
W E Balch
Scripps Research Institute · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BALCH, WILLIAM E · 1993 to 2002
$5.0M
STRUCTURAL AND MOLECULAR ANALYSIS OF CHOROIDEREMIAR01EY011606 · NEI · SCRIPPS RESEARCH INSTITUTE · PI BALCH, WILLIAM EDWARD · 1997 to 2005
$1.6M
NCI NIH HHS CA58689NEI NIH HHS EY11606NEI NIH HHS R01 EY011606
6 · The paper itself

Abstract

Rab escort proteins (REP) 1 and 2 are closely related mammalian proteins required for prenylation of newly synthesized Rab GTPases by the cytosolic heterodimeric Rab geranylgeranyl transferase II complex (RabGG transferase). REP1 in mammalian cells is the product of the choroideremia gene (CHM). CHM/REP1 deficiency in inherited disease leads to degeneration of retinal pigmented epithelium and loss of vision. We now show that amino acid residues required for Rab recognition are critical for function of the yeast REP homologue Mrs6p, an essential protein that shows 50% homology to mammalian REPs. Mutant Mrs6p unable to bind Rabs failed to complement growth of a mrs6Delta null strain and were found to be dominant inhibitors of growth in a wild-type MRS6 strain. Mutants were identified that did not affect Rab binding, yet prevented prenylation in vitro and failed to support growth of the mrs6Delta null strain. These results suggest that in the absence of Rab binding, REP interaction with RabGG transferase is maintained through Rab-independent binding sites, providing a molecular explanation for the kinetic properties of Rab prenylation in vitro. Analysis of the effects of thermoreversible temperature-sensitive (mrs6(ts)) mutants on vesicular traffic in vivo showed prenylation activity is only transiently required to maintain normal growth, a result promising for therapeutic approaches to disease.

Indexed as

Saccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingCell DivisionChoroideremiaCytoplasmFungal ProteinsGenetic Complementation TestGuanine Nucleotide Dissociation InhibitorsIntracellular MembranesModels, MolecularMutagenesisPoint MutationProtein BindingProtein PrenylationProtein Structure, Tertiaryrab GTP-Binding ProteinsAdaptor Proteins, Signal TransducingFungal ProteinsGuanine Nucleotide Dissociation InhibitorsMRS6 protein, S cerevisiaerab GTP-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10893259
PMCPMC2185574
OpenAlexW2067303475

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.