ArticleThe Journal of biological chemistry2013
The p38-interacting protein (p38IP) regulates G2/M progression by promoting α-tubulin acetylation via inhibiting ubiquitination-induced degradation of the acetyltransferase GCN5.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Genome-wide association study of aromatase inhibitor discontinuation due to musculoskeletal symptoms.Supportive care in cancer : official journal of the Multinational Association of Supportive Care in Cancer · 2022Trial
- A narrative review of epigenetic marker in H3K27ac and its emerging potential as a therapeutic target in cancer.Epigenomics · 2025Review
- Epigenetic modulators provide a path to understanding disease and therapeutic opportunity.Genes & development · 2024Review
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- Genome-scale CRISPR-Cas9 screen reveals novel regulators of B7-H3 in tumor cells.Journal for immunotherapy of cancer · 2022Article
- Prediction and analysis of multiple protein lysine modified sites based on conditional wasserstein generative adversarial networks.BMC bioinformatics · 2021Article
- Complex functions of Gcn5 and Pcaf in development and disease.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- The p38-interacting protein p38IP suppresses TCR and LPS signaling by targeting TAK1.EMBO reports · 2020Article
- The regulation of acetylation and stability of HMGA2 via the HBXIP-activated Akt-PCAF pathway in promotion of esophageal squamous cell carcinoma growth.Nucleic acids research · 2020Article
- Article
- Cucurbitacin B exerts anti-cancer activities in human multiple myeloma cells in vitro and in vivo by modulating multiple cellular pathways.Oncotarget · 2017Article
- Supt20 is required for development of the axial skeleton.Developmental biology · 2017Article
- Oncogenic microtubule hyperacetylation through BEX4-mediated sirtuin 2 inhibition.Cell death & disease · 2016Article
- A novel miR-200b-3p/p38IP pair regulates monocyte/macrophage differentiation.Cell discovery · 2016Article
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6 authors at 1 institution in 1 country.
Funding
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Abstract
p38-interacting protein (p38IP) is a component of the GCN5 histone acetyltransferase-containing coactivator complex (GCN5-SAGA complex). It remains unclear whether p38IP or GCN5-SAGA is involved in cell cycle regulation. Using RNA interference to knock down p38IP, we observed that cells were arrested at the G2/M phase, exhibiting accumulation of cyclins, shrunken spindles, and hypoacetylation of α-tubulin. Further analysis revealed that knockdown of p38IP led to proteasome-dependent degradation of GCN5. GCN5 associated with and acetylated α-tubulin, and recovering GCN5 protein levels in p38IP knockdown cells by ectopic expression of GCN5 efficiently reversed α-tubulin hypoacetylation and G2/M arrest. During the G2/M transition, the association of α-tubulin with GCN5 increased, and the acetylation of α-tubulin reached a peak. Biochemical analyses demonstrated that the interaction between p38IP and GCN5 depended on the p38IP N terminus (1-381 amino acids) and GCN5 histone acetyltransferase domain and bromodomain. The p38IP N terminus could effectively reverse p38IP depletion-induced GCN5 degradation, thus recovering α-tubulin acetylation and G2/M progression. p38IP-mediated suppression of GCN5 ubiquitination most likely occurs via nuclear sequestration of GCN5. Our data indicate that the GCN5-SAGA complex is required for G2/M progression, mainly because p38IP promotes the acetylation of α-tubulin by preventing the degradation of GCN5, in turn facilitating the formation of the mitotic spindle.
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