ArticleOncogene2004
MEK1-induced Golgi dynamics during cell cycle progression is partly mediated by Polo-like kinase-3.
Article in Oncogene, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- Article
- The role of polo-like kinase 3 in the response of BRAF-mutant cells to targeted anticancer therapies.Molecular carcinogenesis · 2020Article
- Mechanisms and Regulation of the Mitotic Inheritance of the Golgi Complex.Frontiers in cell and developmental biology · 2015Review
- Polo-like kinases: structural variations lead to multiple functions.Nature reviews. Molecular cell biology · 2014Review
- Roles of Polo-like kinase 3 in suppressing tumor angiogenesis.Experimental hematology & oncology · 2012Article
- Golgi biogenesis.Cold Spring Harbor perspectives in biology · 2011Review
- Plk5, a polo box domain-only protein with specific roles in neuron differentiation and glioblastoma suppression.Molecular and cellular biology · 2011Article
- The Golgi and the centrosome: building a functional partnership.The Journal of cell biology · 2010Review
- Mice deficient in the serine/threonine protein kinase VRK1 are infertile due to a progressive loss of spermatogonia.Biology of reproduction · 2010Article
- Specific phosphorylation and activation of ERK1c by MEK1b: a unique route in the ERK cascade.Genes & development · 2009Article
- Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, a downstream target in a pathway that induces Golgi fragmentation.Molecular and cellular biology · 2009Article
- The Sac1 phosphoinositide phosphatase regulates Golgi membrane morphology and mitotic spindle organization in mammals.Molecular biology of the cell · 2008Article
- Novel genetic tools reveal Cdk5's major role in Golgi fragmentation in Alzheimer's disease.Molecular biology of the cell · 2008Article
- BubR1 deficiency results in enhanced activation of MEK and ERKs upon microtubule stresses.Cell proliferation · 2007Article
- The physiology of membrane transport and endomembrane-based signalling.The EMBO journal · 2006Review
- ERK1c regulates Golgi fragmentation during mitosis.The Journal of cell biology · 2006Article
- Regulation of cell cycle checkpoints by polo-like kinases.Oncogene · 2005Review
- Polo-like kinases in the nervous system.Oncogene · 2005Review
- The Plk3-Cdc25 circuit.Oncogene · 2005Review
- Structure and function of Polo-like kinases.Oncogene · 2005Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
MEK1, a gene product that regulates cell growth and differentiation, also plays an important role in Golgi breakdown during the cell cycle. We have recently shown that polo-like kinase (Plk3) is Golgi localized and involved in Golgi dynamics during the cell cycle. To study the mode of action of Plk3 in the Golgi fragmentation cascade, we examined functional as well as physical interactions between Plk3 and MEK1/ERKs. In HeLa cells, although a significant amount of Plk3 signals dispersed in a manner similar to those of Golgi during mitosis concentrated Plk3 was detected at spindle poles, which colocalized with phospho-MEKs and phospho-ERKs. Pull-down assays showed that Plk3 physically interacted with MEK1 and ERK2. Nocodazole activated Plk3 and its activation was blocked by MEK-specific inhibitors (PD98059 or U0126). Moreover, transfection of activated MEK1 resulted in an enhanced kinase activity of Plk3; Plk3-induced fragmentation of Golgi stacks was significantly reduced after treatment with MEK inhibitors. Consistently, ectopic expression of activated MEK1, but not kinase-dead MEK1(K97R), stimulated Plk3 to induce Golgi breakdown and the stimulation was not observed in cells expressing Plk3(K52R). Furthermore, PLK3(-/-) murine embryonic fibroblast cells exhibited a significantly less fragmentation of the Golgi complex than that in wild-type cells after exposed to nocodazole. Thus, our studies strongly suggest that Plk3 may be a key protein kinase mediating MEK1 function in the Golgi fragmentation pathway during cell division.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.