Alastair Aitken – In Memoriam
The Unit has received the very sad news that Alastair Aitken, a former postdoc in the MRC Protein Phosphorylation Unit has died from pancreatic cancer. Alastair was born in Dundee and left High School at the age of 16 to work in an oil company in the Dundee shipyards. Several years later, he decided to go to University receiving a B.Sc in Chemistry with First Class Honours from Heriot-Watt University, Edinburgh, and an M.Sc in Microbiological Chemistry at the University of Newcastle. He obtained a Ph.D. in the Department of Molecular Biology at the University of Edinburgh under the supervision of Richard Ambler, where he learned how to sequence proteins, and then spent four years at the Institut Pasteur, Paris, initially as a postdoctoral fellow and then as 'Charge de Recherche' in the Division of Virology. He seemed destined to spend the rest of his career at the Institut Pasteur as head of Protein Chemistry. However, a new Director was appointed at Pasteur, who decided that setting up a new protein sequencing facility was not his highest priority and so, much to his surprise and amusement, Alastair found himself back in the town of his birth in late 1978, where Philip Cohen had just obtained the funding to purchase a Beckman Liquid Phase Protein Sequencer, one of a handful of automated protein sequencers in the UK.
The five years that Alastair spent in Philip's lab were highly productive and the 16 papers that Alastair published over this period led to Dundee becoming recognized as Europe's premier location for the identification of phosphorylation sites in proteins. Identifying phosphorylation sites in those days was challenging but, over the period 1980-1982, Alastair managed to identify all the phosphorylation sites on glycogen synthase that were phosphorylated by the protein kinases glycogen synthase kinase 3 (GSK3), cyclic AMP-dependent protein kinase (PKA) and casein kinase 2. This led to glycogen synthase becoming the paradigm for 'multisite phosphorylation'. It also paved the way for the discovery that insulin activates glycogen synthase by inducing dephosphorylation of the sites targeted by GSK3; this in turn led to elucidation of the mechanism by which insulin inhibits GSK3 in the 1990s. Alastair went on identify many serine and threonine residues in proteins that are phosphorylated specifically by PKA or by cyclic GMP-dependent protein kinase (PKG) enhancing our understanding of the similarities and differences in the ways that these protein kinases recognize their substrates. In two further major pieces of work, Alastair determined the entire amino acid sequences of Inhibitor-1 and contributed to the determination of the sequence of inhibitor-2, two specific protein inhibitors of protein phosphatase 1. He also determined the entire amino acid sequence of the B-subunit of calcineurin, a calcium/calmodulin-dependent protein phosphatase. In 1982, Alastair discovered that the N-terminal glycine residue of calcineurin B was blocked with a myristyl group, the same year that Koiti Titani's lab found that the N-terminal glycine residue of PKA was myristylated: these were the first two examples of N-myristoylated proteins.
The outstanding work that Alastair carried out in what was then called the MRC Protein Phosphorylation Group at Dundee, led to his appointment as a Lecturer in the School of Pharmacy at the University of London, and later as a Principal Investigator at the National Institute for Medical Research, London. David Campbell, Alastair's successor in the MRC-PPU said today that he greatly appreciated all the work that Alastair had put into building up an excellent protein chemistry laboratory, something that had made David's job so much easier after he joined us. He also commented that, even after Alastair left Dundee, he was always willing to spend time sharing his experiences and discussing various research problems relating to his time in Dundee.
Alastair returned to Scotland in 1999 as the Professor of Protein Biochemistry at the University of Edinburgh. In his own laboratory, Alastair gained a major international reputation for his pioneering work on the 14-3-3 proteins that interact specifically with phosphorylated motifs in hundreds of proteins. He discovered that the ability of 14-3-3 isoforms to form stable dimers is critical for their regulatory actions, and that the dysregulation of 14-3-3 proteins contributes to CJD, Spinacerebellar ataxia and other neurodegenerative diseases. By generously sharing his reagents with other investigators, and by hosting several extremely successful conferences, Alastair was instrumental in building up a strong community of scientists who are now uncovering an impressive diversity of roles for 14-3-3 proteins in plants and yeast, as well as mammals. His first Ph.D. student was Nick Morrice, who later became the Head of Protein Chemistry in the MRC Protein Phosphorylation Unit setting up and running the Unit's mass spectrometry facility for many years.
Alastair had a passion for science and a real feel for proteins and how they work. He was warm and friendly and made lasting friendships with many other members of the laboratory. He also had a unique and wry sense of humour. With his quiet voice and broad Dundonian accent he could sometimes be difficult to understand and, in reference to the years he had spent in Paris, it was a standing joke in the Unit that Alastair spoke much better French than English, a remark that never failed to bring a smile to his face! Alastair will be sadly missed and we send our condolences to his wife Michele and four children.
The five years that Alastair spent in Philip's lab were highly productive and the 16 papers that Alastair published over this period led to Dundee becoming recognized as Europe's premier location for the identification of phosphorylation sites in proteins. Identifying phosphorylation sites in those days was challenging but, over the period 1980-1982, Alastair managed to identify all the phosphorylation sites on glycogen synthase that were phosphorylated by the protein kinases glycogen synthase kinase 3 (GSK3), cyclic AMP-dependent protein kinase (PKA) and casein kinase 2. This led to glycogen synthase becoming the paradigm for 'multisite phosphorylation'. It also paved the way for the discovery that insulin activates glycogen synthase by inducing dephosphorylation of the sites targeted by GSK3; this in turn led to elucidation of the mechanism by which insulin inhibits GSK3 in the 1990s. Alastair went on identify many serine and threonine residues in proteins that are phosphorylated specifically by PKA or by cyclic GMP-dependent protein kinase (PKG) enhancing our understanding of the similarities and differences in the ways that these protein kinases recognize their substrates. In two further major pieces of work, Alastair determined the entire amino acid sequences of Inhibitor-1 and contributed to the determination of the sequence of inhibitor-2, two specific protein inhibitors of protein phosphatase 1. He also determined the entire amino acid sequence of the B-subunit of calcineurin, a calcium/calmodulin-dependent protein phosphatase. In 1982, Alastair discovered that the N-terminal glycine residue of calcineurin B was blocked with a myristyl group, the same year that Koiti Titani's lab found that the N-terminal glycine residue of PKA was myristylated: these were the first two examples of N-myristoylated proteins.
The outstanding work that Alastair carried out in what was then called the MRC Protein Phosphorylation Group at Dundee, led to his appointment as a Lecturer in the School of Pharmacy at the University of London, and later as a Principal Investigator at the National Institute for Medical Research, London. David Campbell, Alastair's successor in the MRC-PPU said today that he greatly appreciated all the work that Alastair had put into building up an excellent protein chemistry laboratory, something that had made David's job so much easier after he joined us. He also commented that, even after Alastair left Dundee, he was always willing to spend time sharing his experiences and discussing various research problems relating to his time in Dundee.
Alastair returned to Scotland in 1999 as the Professor of Protein Biochemistry at the University of Edinburgh. In his own laboratory, Alastair gained a major international reputation for his pioneering work on the 14-3-3 proteins that interact specifically with phosphorylated motifs in hundreds of proteins. He discovered that the ability of 14-3-3 isoforms to form stable dimers is critical for their regulatory actions, and that the dysregulation of 14-3-3 proteins contributes to CJD, Spinacerebellar ataxia and other neurodegenerative diseases. By generously sharing his reagents with other investigators, and by hosting several extremely successful conferences, Alastair was instrumental in building up a strong community of scientists who are now uncovering an impressive diversity of roles for 14-3-3 proteins in plants and yeast, as well as mammals. His first Ph.D. student was Nick Morrice, who later became the Head of Protein Chemistry in the MRC Protein Phosphorylation Unit setting up and running the Unit's mass spectrometry facility for many years.
Alastair had a passion for science and a real feel for proteins and how they work. He was warm and friendly and made lasting friendships with many other members of the laboratory. He also had a unique and wry sense of humour. With his quiet voice and broad Dundonian accent he could sometimes be difficult to understand and, in reference to the years he had spent in Paris, it was a standing joke in the Unit that Alastair spoke much better French than English, a remark that never failed to bring a smile to his face! Alastair will be sadly missed and we send our condolences to his wife Michele and four children.