A platform for research: civil engineering, architecture and urbanism
A platform for research: civil engineering, architecture and urbanism
Relevance of survivin acetylation for its biological function ; Relevanz der Survivin-Acetylierung für dessen biologische Funktion
Survivin belongs to the inhibitor of apoptosis protein family and is also a regulator of mitosis as it is a member of the chromosomal passenger complex (CPC). While it is not expressed in differentiated adult tissue (Adida et al., 1998), it was found to be upregulated in virtually all types of human cancers (Ambrosini et al., 1997; Adida et al.,2000). Its overexpression is associated with resistance of tumors against chemo- and radiotherapy, frequent recurrences and decreased patient survival (Engels et al., 2007; Capalbo et al., 2007; Xu et al., 2014; Chen et al., 2014). Thus, Survivin is a potential target for cancer therapy. In order to develop strategies for the therapeutic inhibition of Survivin, the mechanisms underlying its dual role have to be clarified in detail. While Survivin fulfills some of its cellular tasks as a homodimer (Pavlyukov et al., 2011), other functions require the monomer (Jeyaprakash et al., 2007). A further layer of complexity is introduced by the fact that Survivin shuttles between the nucleus and the cytoplasm as it is able to passively diffuse into the nucleus and is actively exported by the solublereceptor CRM1 (Rodriguez et al., 2002; Knauer et al., 2006). The mechanisms regulating Survivin’s functions, its localization as well as its dimerization state are still not completely resolved and a matter of scientific disagreement. Recently, Wang et al. (2010b) reported that acetylation of Survivin at lysine 129 facilitates its dimerization, thus causing an accumulation of the protein in the nucleus as only the monomer is able to interact with CRM1 for nuclear export. As lysine acetylation has emerged as a major post-translational modification capable of altering the functions and interactions of proteins, it is conceivable that Survivin’s function might be regulated by the acetylation of any of its 16 lysine residues. Thus, as a preliminary work to our study, which aimed to identify further acetylation sites in Survivin and the effect of a potential acetylation on some of Survivin’s ...
Relevance of survivin acetylation for its biological function ; Relevanz der Survivin-Acetylierung für dessen biologische Funktion
Survivin belongs to the inhibitor of apoptosis protein family and is also a regulator of mitosis as it is a member of the chromosomal passenger complex (CPC). While it is not expressed in differentiated adult tissue (Adida et al., 1998), it was found to be upregulated in virtually all types of human cancers (Ambrosini et al., 1997; Adida et al.,2000). Its overexpression is associated with resistance of tumors against chemo- and radiotherapy, frequent recurrences and decreased patient survival (Engels et al., 2007; Capalbo et al., 2007; Xu et al., 2014; Chen et al., 2014). Thus, Survivin is a potential target for cancer therapy. In order to develop strategies for the therapeutic inhibition of Survivin, the mechanisms underlying its dual role have to be clarified in detail. While Survivin fulfills some of its cellular tasks as a homodimer (Pavlyukov et al., 2011), other functions require the monomer (Jeyaprakash et al., 2007). A further layer of complexity is introduced by the fact that Survivin shuttles between the nucleus and the cytoplasm as it is able to passively diffuse into the nucleus and is actively exported by the solublereceptor CRM1 (Rodriguez et al., 2002; Knauer et al., 2006). The mechanisms regulating Survivin’s functions, its localization as well as its dimerization state are still not completely resolved and a matter of scientific disagreement. Recently, Wang et al. (2010b) reported that acetylation of Survivin at lysine 129 facilitates its dimerization, thus causing an accumulation of the protein in the nucleus as only the monomer is able to interact with CRM1 for nuclear export. As lysine acetylation has emerged as a major post-translational modification capable of altering the functions and interactions of proteins, it is conceivable that Survivin’s function might be regulated by the acetylation of any of its 16 lysine residues. Thus, as a preliminary work to our study, which aimed to identify further acetylation sites in Survivin and the effect of a potential acetylation on some of Survivin’s ...
Relevance of survivin acetylation for its biological function ; Relevanz der Survivin-Acetylierung für dessen biologische Funktion
Unruhe, Britta (author) / Knauer, Shirley K.
2017-12-18
Theses
Electronic Resource
English
| British Library Online Contents | 2013