ArticleMolecular and cellular biology1997
Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 134 citations in OpenAlex.
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- The emerging role of microtubules in invasion plasticity.Frontiers in oncology · 2023Review
- The Calcium/Calmodulin-Dependent Kinases II and IV as Therapeutic Targets in Neurodegenerative and Neuropsychiatric Disorders.International journal of molecular sciences · 2021Review
- A self-organized synthetic morphogenic liposome responds with shape changes to local light cues.Nature communications · 2021Article
- Stathmin Regulates Spatiotemporal Variation in the Memory Loop in Single-Prolonged Stress Rats.Journal of molecular neuroscience : MN · 2020Article
- βPix-d promotes tubulin acetylation and neurite outgrowth through a PAK/Stathmin1 signaling pathway.PloS one · 2020Article
- Interplay Between Calcium and AMPK Signaling in Human Cytomegalovirus Infection.Frontiers in cellular and infection microbiology · 2020Review
- High expression of stathmin 1 is a strong prognostic marker in oral squamous cell carcinoma patients treated by docetaxel-containing regimens.Clinical and experimental medicine · 2017Article
- Deceivingly dynamic: Learning-dependent changes in stathmin and microtubules.Neurobiology of learning and memory · 2015Review
- PIWIL1 destabilizes microtubule by suppressing phosphorylation at Ser16 and RLIM-mediated degradation of Stathmin1.Oncotarget · 2015Article
- Nicotinic acid modulates intracellular calcium concentration and disassembles the cytoskeleton.Molecular medicine reports · 2014Article
- Learning-induced and stathmin-dependent changes in microtubule stability are critical for memory and disrupted in ageing.Nature communications · 2014Article
- Cell type-specific expression of SEPT3-homology subgroup members controls the subunit number of heteromeric septin complexes.Molecular biology of the cell · 2014Article
- IB4-binding sensory neurons in the adult rat express a novel 3' UTR-extended isoform of CaMK4 that is associated with its localization to axons.The Journal of comparative neurology · 2014Article
- 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
- Mammalian SEPT9 isoforms direct microtubule-dependent arrangements of septin core heteromers.Molecular biology of the cell · 2012Article
- Knockdown of PLC-gamma-2 and calmodulin 1 genes sensitizes human cervical adenocarcinoma cells to doxorubicin and paclitaxel.Cancer cell international · 2012Article
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oncoprotein 18 (Op18; also termed p19, 19K, p18, prosolin, and stathmin) is a regulator of microtubule (MT) dynamics and is phosphorylated by multiple kinase systems on four Ser residues. In addition to cell cycle-regulated phosphorylation, external signals induce phosphorylation of Op18 on Ser-25 by the mitogen-activated protein kinase and on Ser-16 by the Ca2+/calmodulin-dependent kinase IV/Gr (CaMK IV/Gr). Here we show that induced expression of a constitutively active mutant of CaMK IV/Gr results in phosphorylation of Op18 on Ser-16. In parallel, we also observed partial degradation of Op18 and a rapid increase of total cellular MTs. These results suggest a link between CaMK IV/Gr, Op18, and MT dynamics. To explore such a putative link, we optimized a genetic system that allowed conditional coexpression of a series of CaMK IV/Gr and Op18 derivatives. The result shows that CaMK IV/Gr can suppress the MT-regulating activity of Op18 by phosphorylation on Ser-16. In line with these results, by employing a chemical cross-linking protocol, it was shown that phosphorylation of Ser-16 is involved in weakening of the interactions between Op18 and tubulin. Taken together, these data suggest that the mechanism of CaMK IV/Gr-mediated suppression of Op18 activity involves both partial degradation of Op18 and direct modulation of the MT-destabilizing activity of this protein. These results show that Op18 phosphorylation by CaMK IV/Gr may couple alterations of MT dynamics in response to external signals that involve Ca2+.
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