Aston Research Centre for Healthy Ageing (ARCHA)
I joined the school of Life and Health Sciences at Aston university as a lecturer in Cell Biology in November 2009 following on from a similar post at Liverpool John Moores University for 2 years (from 2007). It is in the USA that I started being fascinated by the world of Cell Biology when I undertook my postdoctoral studies at the University of Medicine and Dentistry of New Jersey (UMDNJ). It is within these 7 years (2000-2007) that I realised the biological significance of the cellular organisation and their roles in both physiological and diseases states. Prior to this, I received my PhD from the Nottingham Trent University where I graduated in 2000 following on from 3 years of work in the field of Biochemistry. My degrees both from the Nottingham Trent University (applied Biology in 1996) and from Paris XII Creteil (applied biology 1994) were really the steps that took me into the world of science and biology and were the foundations of my career.
The research in our laboratory aims to characterise the role, at the cellular level, of different actin binding/bundling proteins on the organisation of the actin cytoskeleton and the potential roles these proteins may have in disease progressions (such as cancer).
Oncogenic transformation, metastasis, cellular aging and apoptosis are processes where cytoskeleton organization and protein synthesis are often synchronously deregulated. A factor that is essential for regulating both actin remodelling and ribosomal functions is the eukaryotic Elongation Factor 1A (eEF1A). Consequently, and maybe not surprisingly, increases in eEF1A levels have been observed to increase in oncogenic conditions and its level usually correlates to the degree of tumorgenesis. Understanding eEF1A’s non-canonical function towards actin regulation as well as the biological consequences of their interactions on the cytoskeleton and both localised and global protein translation could provide new avenues for therapy in such pathologies. Projects in the lab aim to further determine the importance of the eEF1A-actin interactions on the actin organization in both yeast (saccharomyces cerevisae) and mammalian systems as well as in vitro, using the state of the art facilities in cellular biology and molecular biology offered in our department.
The S100A4 protein has also been linked to cancer progression and has been shown to enhance cellular migration, leading to a metastatic phenotype when it is over expressed in certain tumour cells. Our work and that of others has shown that S100A4 affect the actin cytoskeleton though interaction with the non muscle myosin network. Using cell culture and state of the art facilities in cellular biology and molecular biology, we aim to understand the molecular mechanisms that allow S100A4 to remodel the actin cytoskeleton and the consequences of such reorganisation on cell migration.
2007: Liverpool John Moores University Promising research Scheme. Awarded £25,000. Role of the elongation factor 1 alpha in actin remodelling and cell migration.
Browser does not support script.