Evidence map›Paper›PMID 19956591›Full record

ArticlePloS one2009

The C-terminal sequence of RhoB directs protein degradation through an endo-lysosomal pathway.

Dolores Pérez-Sala, Patricia Boya, Irene Ramos, Mónica Herrera, Konstantinos Stamatakis

Abstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

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  20. Regulating Rho GTPases and their regulators.Nature reviews. Molecular cell biology · 2016
    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

5 authors.

Dolores Pérez-SalaDepartment of Chemical and Physical Biology, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain. dperezsala@cib.csic.es
Patricia Boya
Irene Ramos
Mónica Herrera
Konstantinos Stamatakis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProtein degradation is essential for cell homeostasis. Targeting of proteins for degradation is often achieved by specific protein sequences or posttranslational modifications such as ubiquitination. METHODOLOGY/PRINCIPAL

findingsBy using biochemical and genetic tools we have monitored the localization and degradation of endogenous and chimeric proteins in live primary cells by confocal microscopy and ultra-structural analysis. Here we identify an eight amino acid sequence from the C-terminus of the short-lived GTPase RhoB that directs the rapid degradation of both RhoB and chimeric proteins bearing this sequence through a lysosomal pathway. Elucidation of the RhoB degradation pathway unveils a mechanism dependent on protein isoprenylation and palmitoylation that involves sorting of the protein into multivesicular bodies, mediated by the ESCRT machinery. Moreover, RhoB sorting is regulated by late endosome specific lipid dynamics and is altered in human genetic lipid traffic disease. CONCLUSIONS/SIGNIFICANCE: Our findings characterize a short-lived cytosolic protein that is degraded through a lysosomal pathway. In addition, we define a novel motif for protein sorting and rapid degradation, which allows controlling protein levels by means of clinically used drugs.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCattleEndosomal Sorting Complexes Required for TransportEndosomesGreen Fluorescent ProteinsHumansLipid MetabolismLysosomesMiceMolecular Sequence DataMultivesicular BodiesProtein Sorting SignalsProtein StabilityProtein TransportEndosomal Sorting Complexes Required for TransportGreen Fluorescent ProteinsProtein Sorting SignalsrhoB GTP-Binding Protein

Identifiers

PMID19956591
PMCPMC2780327

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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.