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You searched for subject:(QP552 C96A6). Showing records 1 – 2 of 2 total matches.

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University of St Andrews

1. Angus, Liselotte. Willin as a novel 4.1 ezrin radixin moesin (FERM) domain protein in the mammalian Hippo signalling pathway.

Degree: PhD, 2011, University of St Andrews

The Salvador/Warts/Hippo (Hippo) pathway defines a novel signalling cascade regulating cell contact inhibition, organ size control, cell growth, proliferation, apoptosis and cancer development in mammals. The Hippo pathway was initially utilised in D. melanogaster, where the Expanded protein acts in the Hippo signalling cascade to control organ size. Willin is the proposed human orthologue of Expanded and the aim of this thesis is to investigate whether willin can activate the mammalian Hippo signalling pathway. Ectopic willin expression causes an increase in phosphorylation of the core Hippo signalling pathway components MST1/2, LATS1 and YAP, an effect which can be antagonised by ezrin. In MCF10A cells, willin over-expression antagonises a YAP-induced epithelial-to-mesenchymal transition via the N- terminal FERM (Four-point-one Ezrin Radixin Moesin) domain of willin. Preliminary results show that willin is expressed within the sciatic nerve of rat and mice, and within the neuromast cells in the zebrafish; suggesting that willin and the Hippo pathway may play a vital role in the developmental regulation within the peripheral nervous system. To conclude, willin influences Hippo signalling activity by activating the core Hippo pathway kinase cassette in mammalian cells.

Subjects/Keywords: 612; Willin; Hippo pathway; QP552.C96A6; Cytoskeletal proteins; Gene expression; Cellular signal transduction

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Angus, L. (2011). Willin as a novel 4.1 ezrin radixin moesin (FERM) domain protein in the mammalian Hippo signalling pathway. (Doctoral Dissertation). University of St Andrews. Retrieved from http://hdl.handle.net/10023/2489

Chicago Manual of Style (16th Edition):

Angus, Liselotte. “Willin as a novel 4.1 ezrin radixin moesin (FERM) domain protein in the mammalian Hippo signalling pathway.” 2011. Doctoral Dissertation, University of St Andrews. Accessed July 10, 2020. http://hdl.handle.net/10023/2489.

MLA Handbook (7th Edition):

Angus, Liselotte. “Willin as a novel 4.1 ezrin radixin moesin (FERM) domain protein in the mammalian Hippo signalling pathway.” 2011. Web. 10 Jul 2020.

Vancouver:

Angus L. Willin as a novel 4.1 ezrin radixin moesin (FERM) domain protein in the mammalian Hippo signalling pathway. [Internet] [Doctoral dissertation]. University of St Andrews; 2011. [cited 2020 Jul 10]. Available from: http://hdl.handle.net/10023/2489.

Council of Science Editors:

Angus L. Willin as a novel 4.1 ezrin radixin moesin (FERM) domain protein in the mammalian Hippo signalling pathway. [Doctoral Dissertation]. University of St Andrews; 2011. Available from: http://hdl.handle.net/10023/2489

2. Keays, Maria C. The desaturase gene family : an evolutionary study of putative speciation genes in 12 species of Drosophila.

Degree: PhD, 2011, University of St Andrews

The formation and persistence of species are the subject of much debate among biologists. Many species of Drosophila are behaviourally isolated, meaning that heterospecific individuals are not attracted to one another and do not interbreed. Often, this behavioural isolation is at least in part due to differences in pheromonal preference. Drosophila pheromones are long-chain cuticular hydrocarbons (CHCs). Desaturases are enzymes that are important for the production of CHCs. This thesis investigates the evolution of the gene family across 12 species of Drosophila. Desaturase genes were located in all species. Some genes, those that have previously been shown to have important roles in pheromonal communication, have experienced duplication and loss in several species. Two previously undiscovered duplicates were identified. Generally the desaturase gene family is governed by purifying selection, although following duplication these constraints are relaxed and in some cases duplicated genes show compelling evidence of positive selection. One of the loci under positive selection, the novel duplicate desat1b of the obscura group, was found to have a sex-biased expression pattern and alternative splicing in its 5′ UTR. In RNAi knock-down experiments of desaturase gene function in D. melanogaster, several desaturases were shown to affect CHC profiles of males and females, including some that were previously unlinked to CHC production.

Subjects/Keywords: 591.35; Drosophila; Reproductive isolation; Evolution; Comparative genomics; Natural selection; Expression variation; QL537.D76K4; QP552.C96A6; Drosophila; Comparative genomics; Enzymes; Pheromones

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Keays, M. C. (2011). The desaturase gene family : an evolutionary study of putative speciation genes in 12 species of Drosophila. (Doctoral Dissertation). University of St Andrews. Retrieved from http://hdl.handle.net/10023/2478

Chicago Manual of Style (16th Edition):

Keays, Maria C. “The desaturase gene family : an evolutionary study of putative speciation genes in 12 species of Drosophila.” 2011. Doctoral Dissertation, University of St Andrews. Accessed July 10, 2020. http://hdl.handle.net/10023/2478.

MLA Handbook (7th Edition):

Keays, Maria C. “The desaturase gene family : an evolutionary study of putative speciation genes in 12 species of Drosophila.” 2011. Web. 10 Jul 2020.

Vancouver:

Keays MC. The desaturase gene family : an evolutionary study of putative speciation genes in 12 species of Drosophila. [Internet] [Doctoral dissertation]. University of St Andrews; 2011. [cited 2020 Jul 10]. Available from: http://hdl.handle.net/10023/2478.

Council of Science Editors:

Keays MC. The desaturase gene family : an evolutionary study of putative speciation genes in 12 species of Drosophila. [Doctoral Dissertation]. University of St Andrews; 2011. Available from: http://hdl.handle.net/10023/2478

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