Evidence map›Paper›PMID 16554299›Full record

ArticleThe Journal of biological chemistry2006

Mutations affecting beta-tubulin folding and degradation.

Yaqing Wang, Guoling Tian, Nicholas J Cowan, Fernando Cabral

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Novel loss of function mutation inFrontiers in cellular neuroscience · 2023
    Article
  5. Article
  6. Article
  7. Cardiac microtubules in health and heart disease.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Human mutations that confer paclitaxel resistance.Molecular cancer therapeutics · 2010
    Article
  17. Article
  18. Article
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

4 authors at 2 institutions in 1 country.

Yaqing WangDepartment of Integrative Biology and Pharmacology, The University of Texas Medical School, Houston, Texas 77030.
Guoling TianDepartment of Biochemistry, New York University Medical Center, New York, New York 10016.
Nicholas J CowanDepartment of Biochemistry, New York University Medical Center, New York, New York 10016.
Fernando CabralDepartment of Integrative Biology and Pharmacology, The University of Texas Medical School, Houston, Texas 77030. Electronic address: fcabral@uth.tmc.edu.
Columbia University Irving Medical Center · USThe University of Texas at Austin · US

Funding

TUBULIN MUTATIONS AND PACLITAXEL RESISTANCER01CA085935 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI CABRAL, FERNANDO R · 2000 to 2010
$2.7M
PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLR01DK047234 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI COWAN, NICHOLAS · 1994 to 2005
$2.1M
NCI NIH HHS CA85935NCI NIH HHS R01 CA085935NIDDK NIH HHS DK47234NIDDK NIH HHS R01 DK047234
6 · The paper itself

Abstract

Revertants of a colcemid-resistant Chinese hamster ovary cell line with an altered (D45Y) beta-tubulin have allowed the identification of four cis-acting mutations (L187R, Y398C, a 12-amino acid in-frame deletion, and a C-terminal truncation) that act by destabilizing the mutant tubulin and preventing it from incorporating into microtubules. These unstable beta-tubulins fail to form heterodimers and are predominantly found in association with the chaperonin CCT, suggesting that they cannot undergo productive folding. In agreement with these in vivo observations, we show that the defective beta-tubulins do not stably interact with cofactors involved in the tubulin folding pathway and, hence, fail to exchange with beta-tubulin in purified alphabeta heterodimers. Treatment of cells with MG132 causes an accumulation of the aberrant tubulins, indicating that improperly folded beta-tubulin is degraded by the proteasome. Rapid degradation of the mutant tubulin does not elicit compensatory changes in wild-type tubulin synthesis or assembly. Instead, loss of beta-tubulin from the mutant allele causes a 30-40% decrease in cellular tubulin content with no obvious effect on cell growth or survival.

Indexed as

Protein FoldingAnimalsCHO CellsCricetinaeLeupeptinsMicrotubulesMutationProteasome Endopeptidase ComplexTubulinbenzyloxycarbonylleucyl-leucyl-leucine aldehydeLeupeptinsProteasome Endopeptidase ComplexTubulin

Identifiers

PMID16554299
PMCPMC2715149
OpenAlexW2029445443

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.