ArticleMolecular biology of the cell2008
Global regulation of the interphase microtubule system by abundantly expressed Op18/stathmin.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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.
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.
Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Cell type-specific expression of SEPT3-homology subgroup members controls the subunit number of heteromeric septin complexes.Molecular biology of the cell · 2014Article
- Stathmin and microtubules regulate mitotic entry in HeLa cells by controlling activation of both Aurora kinase A and Plk1.Molecular biology of the cell · 2013Article
- The Microtubule Regulatory Protein Stathmin Is Required to Maintain the Integrity of Axonal Microtubules in Drosophila.PloS one · 2013Article
- Mammalian SEPT9 isoforms direct microtubule-dependent arrangements of septin core heteromers.Molecular biology of the cell · 2012Article
- The microtubule cytoskeleton is required for a G2 cell cycle delay in cancer cells lacking stathmin and p53.Cytoskeleton (Hoboken, N.J.) · 2012Article
- Microtubules support a disk-like septin arrangement at the plasma membrane of mammalian cells.Molecular biology of the cell · 2011Article
- Deciphering the rules governing assembly order of mammalian septin complexes.Molecular biology of the cell · 2011Article
- c-Jun N-terminal kinase phosphorylation of stathmin confers protection against cellular stress.The Journal of biological chemistry · 2010Article
- Functional and spatial regulation of mitotic centromere-associated kinesin by cyclin-dependent kinase 1.Molecular and cellular biology · 2010Article
- Predominant regulators of tubulin monomer-polymer partitioning and their implication for cell polarization.Cellular and molecular life sciences : CMLS · 2009Review
- Stathmin regulates centrosomal nucleation of microtubules and tubulin dimer/polymer partitioning.Molecular biology of the cell · 2009Article
- STAT3-stathmin interactions control microtubule dynamics in migrating T-cells.The Journal of biological chemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Op18/stathmin (Op18), a conserved microtubule-depolymerizing and tubulin heterodimer-binding protein, is a major interphase regulator of tubulin monomer-polymer partitioning in diverse cell types in which Op18 is abundant. Here, we addressed the question of whether the microtubule regulatory function of Op18 includes regulation of tubulin heterodimer synthesis. We used two human cell model systems, K562 and Jurkat, combined with strategies for regulatable overexpression or depletion of Op18. Although Op18 depletion caused extensive overpolymerization and increased microtubule content in both cell types, we did not detect any alteration in polymer stability. Interestingly, however, we found that Op18 mediates positive regulation of tubulin heterodimer content in Jurkat cells, which was not observed in K562 cells. By analysis of cells treated with microtubule-poisoning drugs, we found that Jurkat cells regulate tubulin mRNA levels by a posttranscriptional mechanism similarly to normal primary cells, whereas this mechanism is nonfunctional in K562 cells. We present evidence that Op18 mediates posttranscriptional regulation of tubulin mRNA in Jurkat cells through the same basic autoregulatory mechanism as microtubule-poisoning drugs. This, combined with potent regulation of tubulin monomer-polymer partitioning, enables Op18 to exert global regulation of the microtubule system.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.