Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation
Autor: | Roman Körner, Peter I. Duncan, Patrick Meraldi, Martina Casenghi, Erich A. Nigg, Ulrike Weinhart |
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Rok vydání: | 2003 |
Předmět: |
Xenopus
Centrosome cycle Cell Cycle Proteins macromolecular substances Biology Protein Serine-Threonine Kinases computer.software_genre PLK1 Microtubules Models Biological General Biochemistry Genetics and Molecular Biology Spindle pole body Cell Line Substrate Specificity Microtubule Tubulin Proto-Oncogene Proteins Animals Humans Phosphorylation Molecular Biology Mitosis Microtubule nucleation Glutathione Transferase Centrosome business.industry Nuclear Proteins Microtubule organizing center Cell Biology Recombinant Proteins Cell biology Mutation Artificial intelligence business computer Microtubule-Associated Proteins Protein Kinases Natural language processing Developmental Biology |
Zdroj: | Developmental cell. 5(1) |
ISSN: | 1534-5807 |
Popis: | In animal cells, most microtubules are nucleated at centrosomes. At the onset of mitosis, centrosomes undergo a structural reorganization, termed maturation, which leads to increased microtubule nucleation activity. Centrosome maturation is regulated by several kinases, including Polo-like kinase 1 (Plk1). Here, we identify a centrosomal Plk1 substrate, termed Nlp (ninein-like protein), whose properties suggest an important role in microtubule organization. Nlp interacts with two components of the γ-tubulin ring complex and stimulates microtubule nucleation. Plk1 phosphorylates Nlp and disrupts both its centrosome association and its γ-tubulin interaction. Overexpression of an Nlp mutant lacking Plk1 phosphorylation sites severely disturbs mitotic spindle formation. We propose that Nlp plays an important role in microtubule organization during interphase, and that the activation of Plk1 at the onset of mitosis triggers the displacement of Nlp from the centrosome, allowing the establishment of a mitotic scaffold with enhanced microtubule nucleation activity. |
Databáze: | OpenAIRE |
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