Evidence map›Paper›PMID 20740604›Full record

ArticleCytoskeleton (Hoboken, N.J.)2010

Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity.

Guoling Tian, Simi Thomas, Nicholas J Cowan

Open access · greenAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

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  7. ARF family GTPases with links to cilia.American journal of physiology. Cell physiology · 2020
    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

3 authors at 2 institutions in 1 country.

Guoling TianDepartment of Biochemistry, NYU Langone Medical Center, 550 First Avenue, New York, New York 10016, USA.
Simi Thomas
Nicholas J Cowan
New York University · USNYU Langone Health · US

Funding

Inhibition of the Tubulin Folding Pathway as a Novel Therapy for CancerR01CA121680 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI COWAN, NICHOLAS · 2007 to 2009
$1.1M
NCI NIH HHS CA121680NCI NIH HHS R01 CA121680
6 · The paper itself

Abstract

Assembly of the α/β tubulin heterodimer requires the participation of a series of chaperone proteins (TBCA-E) that function downstream of the cytosolic chaperonin (CCT) as a heterodimer assembly machine. TBCD and TBCE are also capable of acting in a reverse reaction in which they disrupt native heterodimers. Homologs of TBCA-E exist in all eukaryotes, and the amino acid sequences of α- and β-tubulin isotypes are rigidly conserved among vertebrates. However, the efficiency with which TBCD effects tubulin disruption in vivo depends on its origin: bovine (but not human) TBCD efficiently destroys tubulin and microtubules upon overexpression in cultured cells. Here we show that recombinant bovine TBCD is produced in HeLa cells as a stoichiometric cocomplex with β-tubulin, consistent with its behavior in vitro and in vivo. In contrast, expression of human TBCD using the same host/vector system results in the generation of TBCD that is not complexed with β-tubulin. We show that recombinant human TBCD functions indistinguishably from its nonrecombinant bovine counterpart in in vitro CCT-driven folding reactions, in tubulin disruption reactions, and in tubulin GTPase activating protein assays in which TBCD and TBCC stimulate GTP hydrolysis by β-tubulin at a heterodimer concentration far below that required for polymerization into microtubules. We conclude that bovine and human TBCD have functionally identical roles in de novo tubulin heterodimer assembly, and show that the inability of human TBCD to disrupt microtubule integrity upon overexpression in vivo can be overcome by siRNA-mediated suppression of expression of the TBCD regulator Arl2 (ADP ribosylation factor-like protein).

Indexed as

AnimalsCattleGTP-Binding ProteinsHeLa CellsHumansMicrotubule-Associated ProteinsMicrotubulesMolecular ChaperonesProtein ConformationProtein FoldingProtein IsoformsRecombinant ProteinsRNA, Small InterferingTubulinARL2 protein, humanGTP-Binding ProteinsMicrotubule-Associated ProteinsMolecular ChaperonesProtein IsoformsRecombinant ProteinsRNA, Small InterferingTBCD protein, humanTubulin

Identifiers

PMID20740604
PMCPMC2958230
OpenAlexW2045468231

What OpenQuestion holds

Textmetadata
LicenceTDM
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.