Publications by authors named "Melanie Bianca Weisser"
The PP2A-B55 phosphatase regulates a plethora of signaling pathways throughout eukaryotes. How PP2A-B55 selects its substrates presents a severe knowledge gap. By integrating AlphaFold modeling with comprehensive high-resolution mutational scanning, we show that α helices in substrates bind B55 through an evolutionary conserved mechanism.
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- The study investigates how the protein Mrc1 in fission yeast plays a crucial role in the inheritance of histones during DNA replication, which is essential for maintaining epigenetic memory.
- It reveals that mutations in Mrc1 can disrupt the proper segregation of parental histones to the lagging strand, leading to loss of gene silencing.
- The research proposes that Mrc1 is involved in controlling histone recycling between leading and lagging strands, ensuring that both daughter cells receive the necessary epigenetic information.
The PP2A-B55 phosphatase regulates a plethora of signaling pathways throughout eukaryotes. How PP2A-B55 selects its substrates presents a severe knowledge gap. By integrating AlphaFold modelling with comprehensive high resolution mutational scanning, we show that α-helices in substrates bind B55 through an evolutionary conserved mechanism.
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- SARS-CoV-2 interacts with host proteins to enhance viral replication and evade immune responses, with a focus on its NSP3 protein.
- Researchers discovered that NSP3 binds to fragile X mental retardation proteins (FMRPs), and mutations preventing this binding lead to reduced virus replication and lower viral levels in lungs.
- The study highlights how NSP3 disrupts the normal function of FMRPs by competing with another protein, shedding light on both viral mechanisms and potential links to fragile X syndrome.
Viruses interact with numerous host factors to facilitate viral replication and to dampen antiviral defense mechanisms. We currently have a limited mechanistic understanding of how SARS-CoV-2 binds host factors and the functional role of these interactions. Here, we uncover a novel interaction between the viral NSP3 protein and the fragile X mental retardation proteins (FMRPs: FMR1 and FXR1-2).
View Article and Find Full Text PDFProtein phosphatase 2A (PP2A) is an abundant phosphoprotein phosphatase that acts as a tumor suppressor. For this reason, compounds able to activate PP2A are attractive anticancer agents. The compounds iHAP1 and DT-061 have recently been reported to selectively stabilize specific PP2A-B56 complexes to mediate cell killing.
View Article and Find Full Text PDFDynamic protein phosphorylation constitutes a fundamental regulatory mechanism in all organisms. Phosphoprotein phosphatase 4 (PP4) is a conserved and essential nuclear serine and threonine phosphatase. Despite the importance of PP4, general principles of substrate selection are unknown, hampering the study of signal regulation by this phosphatase.
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