ArticleCell cycle (Georgetown, Tex.)2015
Phosphorylation of CHO1 by Lats1/2 regulates the centrosomal activation of LIMK1 during cytokinesis.
Article in Cell cycle (Georgetown, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Integrative machine learning of hypoxia and centrosome-related gene signatures enables prognostic stratification and therapeutic insights in lung adenocarcinoma.Translational cancer research · 2026Article
- The clinicopathological and prognostic significances of LATS1 expression in breast cancer.Histology and histopathology · 2022Article
- LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway.Open medicine (Warsaw, Poland) · 2022Article
- Review
- Ser/Thr kinase Trc controls neurite outgrowth ineLife · 2020Article
- Hippo signaling is intrinsically regulated during cell cycle progression by APC/CProceedings of the National Academy of Sciences of the United States of America · 2019Article
- LATS1 inhibits metastasis and epithelial-mesenchymal transition in head and neck squamous cell carcinoma.International journal of clinical and experimental pathology · 2018Article
- Large tumor suppressors 1 and 2 regulate Aurora-B through phosphorylation of INCENP to ensure completion of cytokinesis.Heliyon · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Large tumor suppressor 1 and 2 (Lats1/2) regulate centrosomal integrity, chromosome segregation and cytokinesis. As components of the centralspindlin complex, the kinesin-like protein CHO1 and its splicing variant MKLP1 colocalize with chromosome passenger proteins and GTPases and regulate the formation of the contractile ring and cytokinesis; however, the regulatory mechanisms of CHO1/MKLP1 remain elusive. Here, we show that Lats1/2 phosphorylate Ser716 in the F-actin-interacting region of CHO1, which is absent in MKLP1. Phosphorylated CHO1 localized to the centrosomes and midbody, and the actin polymerization factor LIM-kinase 1 (LIMK1) was identified as its binding partner. Overexpression of constitutively phosphorylated and non-phosphorylated CHO1 altered the mitotic localization and activation of LIMK1 at the centrosomes in HeLa cells, leading to the inhibition of cytokinesis through excessive phosphorylation of Cofilin and mislocalization of Ect2. These results suggest that Lats1/2 stringently control cytokinesis by regulating CHO1 phosphorylation and the mitotic activation of LIMK1 on centrosomes.
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