Publications by authors named "I Chartrain"

Maternal Embryonic Leucine zipper Kinase (MELK) was recently shown to be involved in cell division of Xenopus embryo epithelial cells. The cytokinetic furrow of these cells ingresses asymmetrically and is developmentally regulated. Two subpopulations of xMELK, the mMELK (for "mitotic" xMELK) and iMELK ("interphase" xMELK), which differ in their spatial and temporal regulation, are detected in Xenopus embryo.

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MELK is a serine/threonine kinase involved in several cell processes, including the cell cycle, proliferation, apoptosis and mRNA processing. However, its function remains elusive. Here, we explored its role in the Xenopus early embryo and show by knockdown that xMELK (Xenopus MELK) is necessary for completion of cell division.

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Article Synopsis
  • - MELK (maternal embryonic leucine zipper kinase) is a protein kinase that plays a critical role in various cellular processes such as cell growth, apoptosis, and the cell cycle, with higher expression levels observed in cancerous cells.
  • - The study reveals that MELK is primarily found in proliferating cells, and its protein levels drop significantly when cells exit the cell cycle, suggesting a link between MELK and cell proliferation.
  • - In experiments using HeLa cells and Xenopus embryos, it was found that about half of MELK is degraded after mitosis, while the other half remains stable during interphase, with its stability during M-phase dependent on phosphorylation.
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ZFPIP (Zinc Finger Pbx1 Interacting Protein) has been recently identified in our laboratory in a yeast two hybrid screen using an embryonic mouse cDNA library and PBX1 as a bait. This gene encodes a large protein (250 kDa) that contains a bipartite NLS, numerous C2H2 zinc fingers and is highly conserved amongst vertebrates. In order to address the role of ZFPIP during embryonic development, we analysed the expression pattern of the gene and performed morpholinos injections into Xenopus laevis embryos.

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MELK is a cell cycle-regulated protein kinase involved in cell cycle progression, proliferation, tumor growth and mRNA splicing. MELK is localized in the cytoplasm and the nucleus during interphase and at the cell cortex during anaphase and telophase. In this report, we show that the regulatory domain of Xenopus MELK when tagged at its C-terminus with the green fluorescent protein (GFP), co-localizes with mitochondria in Xenopus XL2 cells.

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