Dr Hayley Sharpe becomes a tenured group leader

Key points:

• Dr Hayley Sharpe, a group leader in the Institute’s Signalling programme, has been awarded tenure after joining the Institute as a tenure-track group leader in 2019.
• The international referees and expert review panel unanimously recommended the award of tenure in recognition of Hayley’s ground-breaking research and therapeutic potential.

Following tenure review by a committee of Institute and external scientists, Dr Hayley Sharpe has become a permanent group leader in the Institute’s Signalling research programme.

Dr Simon Cook, Institute Director and Head of the Signalling research programme, said: “I’m delighted to congratulate Hayley on her tenure. Since joining the Institute Hayley has enriched our signalling research, collaborating closely with other labs in the programme and across the Institute, and rightly receiving recognition for her research by being selected as an EMBO Young Investigator and becoming a Lister Fellow.  It’s been exciting to see the progress she and her team have made in expanding what we know about how receptor protein tyrosine phosphatases work and are regulated. Her work is ground breaking and promises to provide new insights into the role and regulation of these enigmatic enzymes, with potential for new therapies. These views were echoed by our international referees and expert review panel who unanimously recommended the award of tenure.”

Hayley joined the Institute as a Sir Henry Dale Fellow in 2019, having previously established her independent research group at the Cambridge Institute for Medical Research. The following year she became an EMBO Young Investigator and received a Lister Research Prize Fellowship in recognition of her research performance and the potential of her research to lead to advances in clinical medicine.

Hayley and her team work on proteins in cell membranes that convey information about the external environment of the cell to its interior, playing a role in signalling cascades. Phosphatases alter the function of target proteins by removing phosphate groups. Unlike their counterpart kinases, which act to transfer phosphate groups to proteins, the receptor protein tyrosine phosphatases (RPTPs) are less well understood although they offer significant therapeutic potential. The group’s research focuses on how the cell’s microenvironment influences the activity of RPTPs both in terms of physical properties but also in response to hydrogen peroxide, a chemical messenger in the cell. The team use a combination of approaches, biochemistry, proteomics, cell lines and mice models, to understand the function of RPTPs in health and disease.

In addition to Hayley’s role as a group leader, she is also Chair of the Institute’s equality, diversity and inclusivity programme, equity4success.

Hayley commented: “I’m delighted to have achieved tenure and would like to thank my group and colleagues for their support. The synergies we have with groups across the Institute make it an incredibly stimulating place to be and we’re excited about utilising all the expertise we have here and in the local area to continue to explore how RPTPs work and how we might be able to translate this knowledge for health benefits.”

Career snapshot:

Dr Hayley Sharpe gained her PhD with Dr Sean Munro FRS at the MRC Laboratory of Molecular Biology in Cambridge investigating how transmembrane proteins negotiate the membranes of the secretory pathway. She then moved on to study clinical resistance mechanisms to a Hedgehog pathway inhibitor in skin cancer as a postdoctoral researcher at Genentech, USA, from 2011. In 2016 she started her lab at the Cambridge Institute for Medical Research (CIMR) after obtaining a Wellcome/Royal Society Sir Henry Dale fellowship to focus on cell signalling by receptor tyrosine phosphatases. She joined the Institute in 2019, became an EMBO Young Investigator in 2020 and also received Lister Research Prize fellowship in 2020.

Image description: Polaroid photo-style collage of representations of receptor protein tyrosine phosphatases. Images used from Hay et al. (2023) doi: 10.1016/j.jbc.2022.102750 under a Creative Commons CC-BY license.