Cell cycle transitions depend on protein phosphorylation and dephosphorylation. The discovery of cyclin-dependent kinases (CDKs) and their mode of activation by their cyclin partners explained many important aspects of cell cycle control. As the cell cycle is basically a series of recurrences of a defined set of events, protein phosphatases must obviously be as important as kinases. However, our knowledge about phosphatases lags well behind that of kinases. We still do not know which phosphatase(s) is/are truly responsible for dephosphorylating CDK substrates, and we know very little about whether and how protein phosphatases are regulated. Here, we summarize our present understanding of the phosphatases that are important in the control of the cell cycle and pose the questions that need to be answered as regards the regulation of protein phosphatases.
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http://dx.doi.org/10.1038/embor.2011.263 | DOI Listing |
Cell Div
December 2024
Institute for Research in Immunology and Cancer, Département de biochimie et médecine moléculaire, Université de Montréal, Montreal, Québec, Canada.
Background: Mitosis and cytokinesis are regulated by reversible phosphorylation events controlled by kinases and phosphatases. Drosophila Polo kinase, like its human ortholog PLK1, plays several roles in this process. Multiple mechanisms contribute to regulate Polo/PLK1 activity, localization and interactions.
View Article and Find Full Text PDFDiscov Med
December 2024
Department of Breast Surgery, Jiujiang Maternal and Child Health Hospital, 332000 Jiujiang, Jiangxi, China.
Background: The tumor suppressor wild-type p53 is known for its role in inducing apoptosis in tumor cells. This study investigated the relationship between wild-type p53 and protein phosphatase 1 (PP1) and caspase in promoting apoptosis of breast cancer cells.
Methods: Human breast cancer cell lines MCF-7 and MDA-MB-231 obtained from the American Type Culture Collection were used in this study.
Talanta
December 2024
Marshall Laboratory of Biomedical Engineering, Shenzhen Key Laboratory for Nano-Biosensing Technology, Department of Biomedical Engineering, Medical School, Shenzhen University, Shenzhen, Guangdong, 518060, PR China. Electronic address:
Colorimetric enzyme-linked immunosorbent assays (CELISAs) have long been used for protein biomarker detection in diagnostics. Unfortunately, as confined by the monochromatic nature of detection signals and the limited catalytic activity of enzymes, CELISAs suffer from poor visual resolution and low sensitivity, hindering their effectiveness for early diagnostics in resource-limited settings. Herein, we report an ultrasensitive, high-visual-resolution CELISA (named PE-TSA-AuAg Cage-CELISA) that combines kinetically controlled growth of Ag in AuAg nanocages with poly-enzyme-boosted tyramide signal amplification (PE-TSA), enabling visual semiquantitative detection of protein biomarkers at attomolar levels with the naked eye.
View Article and Find Full Text PDFFront Physiol
December 2024
Department of Internal Medicine, Hypertension and Vascular Research Division, Henry ford hospital, Detroit, MI, United States.
Purpose Of Review: The thick ascending limb (TAL) of loop of Henle is essential for NaCl, calcium and magnesium homeostasis, pH balance and for urine concentration. NKCC2 is the main transporter for NaCl reabsorption in the TAL and its regulation is very complex. There have been recent advancements toward understanding how NKCC2 is regulated by protein trafficking, protein-protein interaction, and phosphorylation/dephosphorylation.
View Article and Find Full Text PDFPLoS Pathog
December 2024
Newcastle University Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
The Hog1 stress-activated protein kinase (SAPK) is a key mediator of stress resistance and virulence in Candida albicans. Hog1 activation via phosphorylation of the canonical TGY motif is mediated by the Pbs2 MAPKK, which itself is activated by the Ssk2 MAPKKK. Although this three-tiered SAPK signalling module is well characterised, it is unclear how Hog1 activation is regulated in response to different stresses.
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