Thesis supervisor: Péter Vilmos
Web address (URL): http://www.brc.hu/gen_drosophila_nuclear_actin.php Location of studies (in Hungarian): BRC, Institute of Genetics – Laboratory of Drosophila Actin Research, Szeged Abbreviation of location of studies: SZBK
Description of the research topic:
Actin is one of the most abundant, multifunctional protein in every eukaryotic cell. Actin itself as well as the numerous actin-binding proteins are major components of the cytoskeleton. Extensive research in the past decade has significantly broadened our view about the role actin plays in the life of the cell and added novel aspects to actin research. One of these new aspects is the discovery of the existence of nuclear actin which became evident only recently. Nuclear activities including transcriptional activation in the case of all three RNA polymerases, editing and nuclear export of mRNAs, and chromatin remodeling all depend on actin. It also became clear that there is a fine-tuned equilibrium between cytoplasmic and nuclear actin pools and that this balance is ensured by an export-import system dedicated to actin. After over half a century of research on conventional actin and its organizing partners in the cytoplasm, it was also an unexpected finding that the nucleus contains more than 30 actin-binding proteins and new classes of actin-related proteins which are not able to form filaments but had evolved nuclear-specific functions.
In the Laboratory of Drosophila Nuclear Actin Research of the Biological Research Centre we investigate the biological significance of this surprising nuclear localization in the case of actin and an actin-binding protein, Moesin. The candidate will participate in the exploration of the nuclear functions of actin. In the first phase of the work he/she will modify the Actin5C gene of Drosophila in different ways to examine the biological significance of the nuclear localization of actin. Next, the candidate will confirm the nuclear functions and the collaborations with interacting partners, such as Moesin, of nuclear actin, by using cell biology techniques, genetic and biochemical methods both in cultured cells and transgenic animals.
Actin is one of the most abundant, multifunctional protein in every eukaryotic cell. Actin itself as well as the numerous actin-binding proteins are major components of the cytoskeleton. Extensive research in the past decade has significantly broadened our view about the role actin plays in the life of the cell and added novel aspects to actin research. One of these new aspects is the discovery of the existence of nuclear actin which became evident only recently. Nuclear activities including transcriptional activation in the case of all three RNA polymerases, editing and nuclear export of mRNAs, and chromatin remodeling all depend on actin. It also became clear that there is a fine-tuned equilibrium between cytoplasmic and nuclear actin pools and that this balance is ensured by an export-import system dedicated to actin. After over half a century of research on conventional actin and its organizing partners in the cytoplasm, it was also an unexpected finding that the nucleus contains more than 30 actin-binding proteins and new classes of actin-related proteins which are not able to form filaments but had evolved nuclear-specific functions.
In the Laboratory of Drosophila Nuclear Actin Research of the Biological Research Centre we investigate the biological significance of this surprising nuclear localization in the case of actin and an actin-binding protein, Moesin. The candidate will participate in the exploration of the nuclear functions of actin. In the first phase of the work he/she will modify the Actin5C gene of Drosophila in different ways to examine the biological significance of the nuclear localization of actin. Next, the candidate will confirm the nuclear functions and the collaborations with interacting partners, such as Moesin, of nuclear actin, by using cell biology techniques, genetic and biochemical methods both in cultured cells and transgenic animals.
Actin is one of the most abundant, multifunctional protein in every eukaryotic cell. Actin itself as well as the numerous actin-binding proteins are major components of the cytoskeleton. Extensive research in the past decade has significantly broadened our view about the role actin plays in the life of the cell and added novel aspects to actin research. One of these new aspects is the discovery of the existence of nuclear actin which became evident only recently. Nuclear activities including transcriptional activation in the case of all three RNA polymerases, editing and nuclear export of mRNAs, and chromatin remodeling all depend on actin. It also became clear that there is a fine-tuned equilibrium between cytoplasmic and nuclear actin pools and that this balance is ensured by an export-import system dedicated to actin. After over half a century of research on conventional actin and its organizing partners in the cytoplasm, it was also an unexpected finding that the nucleus contains more than 30 actin-binding proteins and new classes of actin-related proteins which are not able to form filaments but had evolved nuclear-specific functions.
In the Laboratory of Drosophila Nuclear Actin Research of the Biological Research Centre we investigate the biological significance of this surprising nuclear localization in the case of actin and an actin-binding protein, Moesin. The candidate will participate in the exploration of the nuclear functions of actin. In the first phase of the work he/she will modify the Actin5C gene of Drosophila in different ways to examine the biological significance of the nuclear localization of actin. Next, the candidate will confirm the nuclear functions and the collaborations with interacting partners, such as Moesin, of nuclear actin, by using cell biology techniques, genetic and biochemical methods both in cultured cells and transgenic animals. http://www.brc.hu/gen_drosophila_nuclear_actin.php?change_lang=en
Required language skills: English Recommended language skills (in Hungarian): English Further requirements: Participation on the TDK conference
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