The 2008 Applied Biosystems Edman Award: Mark Graham

Children's Medical Research Institute

Graham Mark Graham graduated from the University of Newcastle with a double major in chemistry in 1996 and an Honours degree in 1997. For Honours, Mark studied gas phase clusters of carbon dioxide and nitrous oxide. This involved the modification and optimisation of a purpose-built time-of-flight mass spectrometer in the hope of finding novel stable structures in the same vein as 'bucky balls'. Mark can report that condensed carbon dioxide and nitrous oxide have quite amorphous structures. Mark continued research at the University of Newcastle for his PhD (awarded 2002), jointly supervised by Ellak von Nagy-Felsobuki and Peter Dunkley. At this time, he switched focus from chemistry to biomedical research. He studied the phosphorylation of tyrosine hydroxylase, the rate-limiting enzyme in the synthesis of adrenaline and noradrenaline. His work explained how multi-site phosphorylation could regulate enzyme activity in a kinetic analysis using quantitative mass spectrometry. Mark moved to the Children's Medical Research Institute (CMRI), at Westmead in Sydney, in 2002 as a postdoctoral fellow under Phillip Robinson. Mark's position is now senior research officer at CMRI with a conjoint appointment as senior lecturer at the University of Sydney.

At CMRI, Mark focused on neuroscience and cancer research, with an interest in protein phosphorylation. A highlight of his work includes working as part of the team that identified the kinase responsible for phosphorylating dynamin I, a key protein in synaptic vesicle endocytosis. He also contributed to the discovery of the phospho-regulated binding partner for dynamin I. He led the project that determined the seven dynamin I in vivo phosphorylation sites and ranked them according to their importance in endocytosis. The splice variants of dynamin I are now under further analysis. He worked with Martin Lavin's team at the Queensland Institute for Medical Research to determine in vivo phosphorylation sites on ATM kinase, a key protein in the DNA damage response. With Roger Reddel's team at CMRI, he identified the components of the telomerase complex, which was published in Science. Mark also contributed to methods for studying protein phosphorylation using mass spectrometry. He demonstrated the usefulness of intact phosphoprotein analysis and graphite capture of short hydrophilic phosphopeptides. He is currently leading a project on AP180, a protein that regulates the quantal size of synaptic vesicles. He has discovered a novel post-translational modification on AP180, which is now the subject of a Mizutani Foundation for Glycoscience grant awarded in 2008.

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This page last modified: July 15, 2008.