Abstract
Ezrin-Radixin-Moesin (ERM) proteins play an essential role in the cytoplasm by cross-linking actin filaments with plasma membrane proteins. Research has identified the nuclear localization of ERMs, as well as the involvement of a single Drosophila ERM protein, Moesin, in nuclear mRNA exports. However, the question of how important the nuclear activity of ERM proteins are for the life of an organism has so far not been explored. Here, we present the first attempt to reveal the invivo relevance of nuclear localization of Moesin in Drosophila. With the help of a nuclear export signal, we decreased the amount of Moesin in the nuclei of the animals. Furthermore, we observed various developmental defects, demonstrating the importance of ERM function in the nucleus for the first time. Transcriptome analysis of the mutant flies revealed that the lack of nuclear Moesin function leads to expression changes in nearly 700 genes, among them heat-shock genes. This result together with additional findings revealed that in Drosophila the expression ofprotein chaperones requires the nuclear functions of Moesin. DATABASE: GEO accession number: GSE155778.
Highlights
The presence of cytoskeletal proteins in the nucleus is undisputed today, and it is clear that they are involved in fundamental nuclear functions [1,2,3,4]
The FEBS Journal published by John Wiley & Ltd on behalf of Federation of European Biochemical Societies
In Drosophila, the moe gene is located on the X chromosome and with the use of alternative START sites and introns it encodes 13 different transcripts that give rise to seven different protein isoforms
Summary
The presence of cytoskeletal proteins in the nucleus is undisputed today, and it is clear that they are involved in fundamental nuclear functions [1,2,3,4]. The biological relevance of the activity of cytoskeletal proteins in the nucleus has not yet been determined and is still debated. This is primarily due to the fact that cytoskeletal proteins have essential activities in the cytoplasm, and the elimination or inhibition of these proteins affects their activity in the cytoplasm as well. The FEBS Journal 288 (2021) 4812–4832 a 2021 The Authors. The FEBS Journal published by John Wiley & Ltd on behalf of Federation of European Biochemical Societies
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