Evidence map›Paper›PMID 23716697›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Molecular mechanism and functional role of brefeldin A-mediated ADP-ribosylation of CtBP1/BARS.

Antonino Colanzi, Giovanna Grimaldi, Giuliana Catara, Carmen Valente, Claudia Cericola, Prisca Liberali, Maurizio Ronci, Vasiliki S Lalioti, Agostino Bruno, Andrea R Beccari and 6 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-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

23 citing papers in PubMed, 87 citations in OpenAlex.

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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

16 authors at 10 institutions in 3 countries.

Antonino ColanziInstitute of Protein Biochemistry, National Research Council, 80131 Naples, Italy. a.colanzi@ibp.cnr.it
Giovanna Grimaldi
Giuliana Catara
Carmen Valente
Claudia Cericola
Prisca Liberali
Maurizio Ronci
Vasiliki S Lalioti
Agostino Bruno
Andrea R Beccari
Andrea Urbani
Antonio De Flora
Marco Nardini
Martino Bolognesi
Alberto Luini
Daniela Corda
National Academies of Sciences, Engineering, and Medicine · USInstitute of Protein Biochemistry · ITMario Negri Sud Foundation · ITUniversity of Milan · ITUniversity of Parma · ITFondazione Santa Lucia · ITNational Research Council · ITUniversidad Autónoma de Madrid · ESUniversity of Genoa · ITUniversity of Rome Tor Vergata · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP-ribosylation is a posttranslational modification that modulates the functions of many target proteins. We previously showed that the fungal toxin brefeldin A (BFA) induces the ADP-ribosylation of C-terminal-binding protein-1 short-form/BFA-ADP-ribosylation substrate (CtBP1-S/BARS), a bifunctional protein with roles in the nucleus as a transcription factor and in the cytosol as a regulator of membrane fission during intracellular trafficking and mitotic partitioning of the Golgi complex. Here, we report that ADP-ribosylation of CtBP1-S/BARS by BFA occurs via a nonconventional mechanism that comprises two steps: (i) synthesis of a BFA-ADP-ribose conjugate by the ADP-ribosyl cyclase CD38 and (ii) covalent binding of the BFA-ADP-ribose conjugate into the CtBP1-S/BARS NAD(+)-binding pocket. This results in the locking of CtBP1-S/BARS in a dimeric conformation, which prevents its binding to interactors known to be involved in membrane fission and, hence, in the inhibition of the fission machinery involved in mitotic Golgi partitioning. As this inhibition may lead to arrest of the cell cycle in G2, these findings provide a strategy for the design of pharmacological blockers of cell cycle in tumor cells that express high levels of CD38.

Indexed as

Adenosine Diphosphate RiboseADP-ribosyl CyclaseADP-ribosyl Cyclase 1Alcohol OxidoreductasesAnimalsBinding, CompetitiveBinding SitesBlotting, WesternBrefeldin ACytosolDNA-Binding ProteinsHeLa CellsHumansMembrane GlycoproteinsModels, MolecularNADAdenosine Diphosphate RiboseADP-ribosyl CyclaseADP-ribosyl Cyclase 1Alcohol OxidoreductasesBrefeldin ACD38 protein, humanC-terminal binding proteinDNA-Binding ProteinsMembrane GlycoproteinsNADanticancer moleculescell signalingGolgi fragmentationmitosis

Identifiers

PMID23716697
PMCPMC3683763
OpenAlexW1979406565

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.