ArticleThe Journal of cell biology1998
Regulation of microtubule dynamics by extracellular signals: cAMP-dependent protein kinase switches off the activity of oncoprotein 18 in intact cells.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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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.
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Who cites it
35 citing papers in PubMed, 140 citations in OpenAlex.
- Inhibitors of phosphodiesterase 1 enhance paclitaxel cytotoxicity in a MDA-MB-231-derived cell line by promoting microtubule stabilization.BBA advances · 2026Article
- Molecular interactions at the colchicine binding site in tubulin: An X-ray crystallography perspective.Drug discovery today · 2022Review
- Stathmin dynamics modulate the activity of eribulin in breast cancer cells.Pharmacology research & perspectives · 2021Article
- Stathmin Regulates Spatiotemporal Variation in the Memory Loop in Single-Prolonged Stress Rats.Journal of molecular neuroscience : MN · 2020Article
- PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of Stathmin1.Oncotarget · 2015Article
- Role of microtubules in attenuation of PepG-induced vascular endothelial dysfunction by atrial natriuretic peptide.Biochimica et biophysica acta · 2015Article
- SIAH ubiquitin ligases regulate breast cancer cell migration and invasion independent of the oxygen status.Cell cycle (Georgetown, Tex.) · 2015Article
- cAMP-dependent protein kinase and c-Jun N-terminal kinase mediate stathmin phosphorylation for the maintenance of interphase microtubules during osmotic stress.The Journal of biological chemistry · 2014Article
- Novel role of stathmin in microtubule-dependent control of endothelial permeability.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Stathmin is dispensable for tumor onset in mice.PloS one · 2012Article
- Protein kinase A-mediated serine 35 phosphorylation dissociates histone H1.4 from mitotic chromosome.The Journal of biological chemistry · 2011Article
- Deciphering the rules governing assembly order of mammalian septin complexes.Molecular biology of the cell · 2011Article
- Excessive ovarian production of nerve growth factor elicits granulosa cell apoptosis by setting in motion a tumor necrosis factor α/stathmin-mediated death signaling pathway.Reproduction (Cambridge, England) · 2011Article
- Phosphorylation controls autoinhibition of cytoplasmic linker protein-170.Molecular biology of the cell · 2010Article
- The p38/MAPK pathway regulates microtubule polymerization through phosphorylation of MAP4 and Op18 in hypoxic cells.Cellular and molecular life sciences : CMLS · 2010Article
- Predominant regulators of tubulin monomer-polymer partitioning and their implication for cell polarization.Cellular and molecular life sciences : CMLS · 2009Review
- Regulation of microtubule dynamic instability in vitro by differentially phosphorylated stathmin.The Journal of biological chemistry · 2009Article
- Autonomous turning of cerebellar granule cells in vitro by intrinsic programs.Developmental biology · 2009Article
- Global regulation of the interphase microtubule system by abundantly expressed Op18/stathmin.Molecular biology of the cell · 2008Article
- Interphase-specific phosphorylation-mediated regulation of tubulin dimer partitioning in human cells.Molecular biology of the cell · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oncoprotein 18 (Op18, also termed p19, 19K, metablastin, stathmin, and prosolin) is a recently identified regulator of microtubule (MT) dynamics. Op18 is a target for both cell cycle and cell surface receptor-coupled kinase systems, and phosphorylation of Op18 on specific combinations of sites has been shown to switch off its MT-destabilizing activity. Here we show that induced expression of the catalytic subunit of cAMP-dependent protein kinase (PKA) results in a dramatic increase in cellular MT polymer content concomitant with phosphorylation and partial degradation of Op18. That PKA may regulate the MT system by downregulation of Op18 activity was evaluated by a genetic system allowing conditional co-expression of PKA and a series of kinase target site-deficient mutants of Op18. The results show that phosphorylation of Op18 on two specific sites, Ser-16 and Ser-63, is necessary and sufficient for PKA to switch off Op18 activity in intact cells. The regulatory importance of dual phosphorylation on Ser-16 and Ser-63 of Op18 was reproduced by in vitro assays. These results suggest a simple model where PKA phosphorylation downregulates the MT-destabilizing activity of Op18, which in turn promotes increased tubulin polymerization. Hence, the present study shows that Op18 has the potential to regulate the MT system in response to external signals such as cAMP-linked agonists.
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