Publications by authors named "P Vilmos"
Article Synopsis
- The lymph gland in Drosophila larvae serves as a model for understanding blood cell development, featuring different zones responsible for progenitor and differentiated hemocyte functions.
- Previous studies indicated that the Headcase (Hdc) factor is crucial for controlling hemocyte differentiation in this organ, but how it operates at the molecular level was unclear until now.
- The current study reveals that Hdc regulates differentiation by inhibiting the insulin/mTOR signaling pathway, impacting both the niche environment and the progenitor cells autonomously, thereby providing insights into blood stem cell maintenance that could apply to vertebrates.
Article Synopsis
- The ERM protein family, including Moesin, plays crucial roles in cellular activities, traditionally known for their functions in the cytoplasm, but they've also been implicated in nuclear processes.
- The study identified that Moesin directly interacts with the Mediator complex, specifically its Med15 subunit, and that both proteins are essential for proper gene expression related to heat shock response.
- Moesin, Med15, and heat shock factor (Hsf) form a nuclear complex that includes the monomeric form of actin, providing insight into the mechanisms by which ERM proteins function in the nucleus and highlighting the evolutionary importance of this interaction.
The ERM protein family, which consists of three closely related proteins in vertebrates, ezrin, radixin, and moesin (ERM), is an ancient and important group of cytoplasmic actin-binding and organizing proteins. With their FERM domain, ERMs bind various transmembrane proteins and anchor them to the actin cortex through their C-terminal F-actin binding domain, thus they are major regulators of actin dynamics in the cell. ERMs participate in many fundamental cellular processes, such as phagocytosis, microvilli formation, T-cell activation and tumor metastasis.
View Article and Find Full Text PDFThe FERM domain is a conserved and widespread protein module that appeared in the common ancestor of amoebae, fungi, and animals, and is therefore now found in a wide variety of species. The primary function of the FERM domain is localizing to the plasma membrane through binding lipids and proteins of the membrane; thus, for a long time, FERM domain-containing proteins (FDCPs) were considered exclusively cytoskeletal. Although their role in the cytoplasm has been extensively studied, the recent discovery of the presence and importance of cytoskeletal proteins in the nucleus suggests that FDCPs might also play an important role in nuclear function.
View Article and Find Full Text PDFThe conserved Ser/Thr protein phosphatase 5 (PP5) is involved in the regulation of key cellular processes, including DNA damage repair and cell division in eukaryotes. As a co-chaperone of Hsp90, PP5 has been shown to modulate the maturation and activity of numerous oncogenic kinases. Here, we identify a novel substrate of PP5, the Polo-like kinase 4 (Plk4), which is the master regulator of centriole duplication in animal cells.
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