Evidence map›Paper›PMID 20676133›Full record

ArticleOncogene2010

Multiple modification and protein interaction signals drive the Ring finger protein 11 (RNF11) E3 ligase to the endosomal compartment.

E Santonico, F Belleudi, S Panni, M R Torrisi, G Cesareni, L Castagnoli

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In one paragraph

Article in Oncogene, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. [Mechanism of ring finger protein 11 regulating Akt signaling pathway to promote osteogenic differentiation of bone marrow mesenchymal stem cells].Zhongguo xiu fu chong jian wai ke za zhi = Zhongguo xiufu chongjian waike zazhi = Chinese journal of reparative and reconstructive surgery · 2022
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  17. Regulation of NF-κB signaling by the A20 deubiquitinase.Cellular & molecular immunology · 2012
    Review
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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

6 authors at 5 institutions in 1 country.

E SantonicoDepartment of Molecular Biology, Tor Vergata University of Rome, Rome, Italy. Elena.Santonico@uniroma2.it
F Belleudi
S Panni
M R Torrisi
G Cesareni
L Castagnoli
University of Rome Tor Vergata · ITAzienda Ospedaliera Sant'Andrea · ITFondazione Santa Lucia · ITIstituto Pasteur · ITUniversity of Calabria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ring finger protein 11 (RNF11) is a small RING E3-ligase overexpressed in numerous human prostate, colon and invasive breast cancers. Although functional studies have implicated RNF11 in a variety of biological processes, including signal transduction and apoptosis, the molecular mechanisms underlying its function are still poorly understood. In this study we show that RNF11 is a membrane-associated E3 ligase co-localizing with markers of both the early and the recycling endosomes. Several modification and protein interaction signals in the RNF11 sequence are shown to affect its compartmentalization. Membrane binding requires two acylation motifs driving the myristoylation of Gly2 and the S-palmitoylation of Cys4. Accordingly, genetic removal of the myristoylating signal results in diffuse staining, whereas an RNF11 protein mutated in the palmitoylation signal is retained in compartments of the early secretory pathway. However, amino-terminal fusion to green fluorescent protein of a 10-residue peptide containing both acylation signals re-localizes the chimera to the plasma membrane, but it is not sufficient to direct it to the recycling compartment suggesting that additional signals contribute to the correct localization. In addition, we show that membrane anchoring through acylation is necessary for RNF11 to be post-translationally modified by the addition of several ubiquitin moieties and that loss of acylation severely impairs the in vivo ubiquitination mediated by the HECT E3-ligases Itch and Nedd4. Finally, in cells transfected with RNF11 we observe a correlation between high RNF11 expression, as in tumor cells, and a swelling of the endosomal compartment suggesting a possible role of the dysregulation of the endosome compartment in tumorigenesis.

Indexed as

Signal TransductionAcylationBlotting, WesternCarrier ProteinsCell LineDNA-Binding ProteinsEndosomesGreen Fluorescent ProteinsHeLa CellsHumansMembrane ProteinsMicroscopy, FluorescenceProtein BindingRecombinant Fusion ProteinsTransfectionUbiquitinationCarrier ProteinsDNA-Binding ProteinsGreen Fluorescent ProteinsMembrane ProteinsRecombinant Fusion ProteinsRNF11 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID20676133
OpenAlexW1970495391

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.