Evidence map›Paper›PMID 20204449›Full record

ArticleCellular and molecular life sciences : CMLS2010

Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress.

Olga Voloshin, Yana Gocheva, Marina Gutnick, Natalia Movshovich, Anya Bakhrat, Keren Baranes-Bachar, Dudy Bar-Zvi, Ruti Parvari, Larisa Gheber, Dina Raveh

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Mechanisms controlling neuromuscular junction stability.Cellular and molecular life sciences : CMLS · 2015
    Review
  7. Article
  8. Autoinhibition of TBCB regulates EB1-mediated microtubule dynamics.Cellular and molecular life sciences : CMLS · 2013
    Article
  9. Review
  10. Article
  11. Article
  12. Faithful chaperones.Cellular and molecular life sciences : CMLS · 2011
    Review
  13. 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

10 authors at 1 institution in 1 country.

Olga VoloshinDepartment of Life Sciences, Ben Gurion University of the Negev, P.O. Box 653, 84105, Beersheba, Israel.
Yana Gocheva
Marina Gutnick
Natalia Movshovich
Anya Bakhrat
Keren Baranes-Bachar
Dudy Bar-Zvi
Ruti Parvari
Larisa Gheber
Dina Raveh
Ben-Gurion University of the Negev · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutation of tubulin chaperone E (TBCE) underlies hypoparathyroidism, retardation, and dysmorphism (HRD) syndrome with defective microtubule (MT) cytoskeleton. TBCE/yeast Pac2 comprises CAP-Gly, LRR (leucine-rich region), and UbL (ubiquitin-like) domains. TBCE folds alpha-tubulin and promotes alpha/beta dimerization. We show that Pac2 functions in MT dynamics: the CAP-Gly domain binds alpha-tubulin and MTs, and functions in suppression of benomyl sensitivity of pac2Delta mutants. Pac2 binds proteasomes: the LRR binds Rpn1, and the UbL binds Rpn10; the latter interaction mediates Pac2 turnover. The UbL also binds the Skp1-Cdc53-F-box (SCF) ubiquitin ligase complex; these competing interactions for the UbL may impact on MT dynamics. pac2Delta mutants are sensitive to misfolded protein stress. This is suppressed by ectopic PAC2 with both the CAP-Gly and UbL domains being essential. We propose a novel role for Pac2 in the misfolded protein stress response based on its ability to interact with both the MT cytoskeleton and the proteasomes.

Indexed as

Molecular ChaperonesAmino Acid SequenceCell Cycle ProteinsCytoskeletonDimerizationF-Box ProteinsF-Box-WD Repeat-Containing Protein 7HumansHypoparathyroidismIntellectual DisabilityIntracellular Signaling Peptides and ProteinsMicrotubulesMutationProteasome Endopeptidase ComplexProteinsSyndromeCell Cycle ProteinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanIntracellular Signaling Peptides and ProteinsLGI1 protein, humanMolecular ChaperonesProteasome Endopeptidase ComplexProteinsTubulinUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID20204449
PMCPMC11115895
OpenAlexW2041519111

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.