ArticleMolecular and cellular biology1996
Constitutive expression of murine Sak-a suppresses cell growth and induces multinucleation.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 76 citations in OpenAlex.
- Role of PLK4 inhibition in cancer therapy.Cancer metastasis reviews · 2025Review
- Polo-like kinase 4 homodimerization and condensate formation regulate its own protein levels but are not required for centriole assembly.Molecular biology of the cell · 2023Article
- Global cellular response to chemical perturbation of PLK4 activity and abnormal centrosome number.eLife · 2022Article
- Polo-Like Kinase 4's Critical Role in Cancer Development and Strategies for Plk4-Targeted Therapy.Frontiers in oncology · 2021Review
- FAM46C/TENT5C functions as a tumor suppressor through inhibition of Plk4 activity.Communications biology · 2020Article
- Polo-Like Kinase 4 (PLK4) Is Overexpressed in Central Nervous System Neuroblastoma (CNS-NB).Bioengineering (Basel, Switzerland) · 2018Article
- PLK4 phosphorylation of CP110 is required for efficient centriole assembly.Cell cycle (Georgetown, Tex.) · 2017Article
- DNA replication licensing factor Cdc6 and Plk4 kinase antagonistically regulate centrosome duplication via Sas-6.Nature communications · 2017Article
- Loss of KLF14 triggers centrosome amplification and tumorigenesis.Nature communications · 2015Article
- Targeting Polo-Like Kinases: A Promising Therapeutic Approach for Cancer Treatment.Translational oncology · 2015Review
- Two Polo-like kinase 4 binding domains in Asterless perform distinct roles in regulating kinase stability.The Journal of cell biology · 2015Article
- Polo-like kinase 4 transcription is activated via CRE and NRF1 elements, repressed by DREAM through CDE/CHR sites and deregulated by HPV E7 protein.Nucleic acids research · 2014Article
- Centrosome amplification causes microcephaly.Nature cell biology · 2013Article
- Show me your license, please: deregulation of centriole duplication mechanisms that promote amplification.Cellular and molecular life sciences : CMLS · 2013Review
- SmSak, the second Polo-like kinase of the helminth parasite Schistosoma mansoni: conserved and unexpected roles in meiosis.PloS one · 2012Article
- Downregulation of polo-like kinase 4 in hepatocellular carcinoma associates with poor prognosis.PloS one · 2012Article
- Mitotic Kinases and p53 Signaling.Biochemistry research international · 2012Article
- The Protein Phosphatase 2A regulatory subunit Twins stabilizes Plk4 to induce centriole amplification.The Journal of cell biology · 2011Article
- Male hypogonadism and germ cell loss caused by a mutation in Polo-like kinase 4.Endocrinology · 2011Article
- Centrosome amplification in CHO and DT40 cells by inactivation of cyclin-dependent kinases.Cytoskeleton (Hoboken, N.J.) · 2011Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The murine Sak gene encodes two isoforms of a putative serine/threonine kinase, Sak-a and Sak-b, with a common N-terminal kinase domain and different C-terminal sequences. Sak is expressed primarily at sites where cell division is most active in adult and embryonic tissues (C. Fode, B. Motro, S. Youseli, M. Heffernan, and J. W. Dennis, Proc. Natl. Acad. Sci. USA 91:6388-6392, 1994). In this study, we found that Sak-a transcripts were absent in growth-arrested NIH 3T3 cells, while in cycling cells, mRNA levels increased late in G1 phase and remained elevated through S phase and mitosis before declining early in G1. The half-life of hemagglutinin epitope-tagged Sak-a protein was determined to be approximately 2 to 3 h, and the protein was observed to be multiubiquitinated, a signal for rapid protein degradation. Overexpression of Sak-a protein inhibited colony-forming efficiency in CHO cells. Neither the Sak-b isoform nor Sak-a with a mutation in a strictly conserved residue in the kinase domain (Asp-154-->Asn) conferred growth inhibition, suggesting that both the kinase domain and the C-terminal portion of Sak-a are functional regions of the protein. Sak-a overexpression did not induce a block in the cell cycle. However, expression of HA-Sak-a, but not HA-Sak-b, from a constitutive promoter for 48 h in CHO cells increased the incidence of multinucleated cells. Our results show that Sak-a transcript levels are controlled in a cell cycle-dependent manner and that this precise regulation is necessary for cell growth and the maintenance of nuclear integrity during cell division.
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