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Nuclear Transport Signals in the proteins of the ARP2/3 complex
Němcová, Barbora ; Bellinvia, Erica (advisor) ; Cvrčková, Fatima (referee)
The intracellular movement of macromolecules such as proteins and RNA is essential for maintaining cellular homeostasis and coordinating various cellular processes. In eukaryotic cells, the transport of these molecules between the cytoplasm and the nucleus is carefully regulated. Nuclear transport signals (NTS) play a key role in facilitating the import and export of proteins across the nuclear envelope. The ARP2/3 complex, which is an important regulator of activity dynamics, has been studied mainly for its functions in the cytoplasm, such as cell movement and cell division. However, new findings suggest that the ARP2/3 complex might also have nuclear functions in plants. Plants are unique multicellular organisms that rely on precisely coordinated cellular activities for growth, development, and response to stimuli. Understanding the molecular mechanisms behind nuclear processes in plants has recently become a focus of research. The ARP2/3 complex, which consists of seven subunits, is known for its ability to branch actin filaments and thereby control cellular processes requiring actin remodeling. However, recent studies have revealed a potential link between the ARP2/3 complex and nuclear functions in plants. Proteins associated with the ARP2/3 complex have been found to localize within the plant...
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Interactions of polyomavirus structures in the endoplasmic reticulum and on the path to the nucleus
Svobodová, Terezie ; Huerfano Meneses, Sandra (advisor) ; Weber, Jan (referee)
Mouse polyomavirus is a member and model virus of Polyomaviridae family. In order to infect cells and produce viral progeny, the viral chromosome must be transported to the nucleus. Several studies suggest that virions are transporeted to the endoplasmic reticulum, from which they are transferred to the cytosol with assistace of host proteins. Two of these proteins are the chaperon, BiP (binding immunoglobulin protein) and the cochaperone, DNAJ B14. Polyomaviruses probably enter the nucleus through nuclear pores with the assistence of importins. These processes were mainly studied with SV40. In this work, we show that MPyV infection induces a change in distribution of the DNAJ B14 protein, which became clustered into foci, where it co-localizes with the viral capsid protein, VP1. The occurrence of foci varies during infection. With use of proximity ligation assay, we have shown that during an early fase of MPyV infection, DNAJ B14 and BiP get in the close proximity with VP1. It is suggested that negatively charged amino acids at the N-terminus of the minor capsid protein, VP2, are required for targeting virions to translocon and proteins associated with ERAD. We created MPyV with VP2 mutated in these amino acids. The negatively charged amino acid at position 17 is not necessary for successful...
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Interactions of polyomavirus structures in the endoplasmic reticulum and on the path to the nucleus
Svobodová, Terezie ; Huerfano Meneses, Sandra (advisor) ; Weber, Jan (referee)
Mouse polyomavirus is a member and model virus of Polyomaviridae family. In order to infect cells and produce viral progeny, the viral chromosome must be transported to the nucleus. Several studies suggest that virions are transporeted to the endoplasmic reticulum, from which they are transferred to the cytosol with assistace of host proteins. Two of these proteins are the chaperon, BiP (binding immunoglobulin protein) and the cochaperone, DNAJ B14. Polyomaviruses probably enter the nucleus through nuclear pores with the assistence of importins. These processes were mainly studied with SV40. In this work, we show that MPyV infection induces a change in distribution of the DNAJ B14 protein, which became clustered into foci, where it co-localizes with the viral capsid protein, VP1. The occurrence of foci varies during infection. With use of proximity ligation assay, we have shown that during an early fase of MPyV infection, DNAJ B14 and BiP get in the close proximity with VP1. It is suggested that negatively charged amino acids at the N-terminus of the minor capsid protein, VP2, are required for targeting virions to translocon and proteins associated with ERAD. We created MPyV with VP2 mutated in these amino acids. The negatively charged amino acid at position 17 is not necessary for successful...
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