Prof. Matthias Hentze

Biography

Matthias Hentze Director Professor Matthias Hentze was born in Rheda-Wiedenbrück, Germany. He attended Münster University Medical School, Germany, and also studied at Medical Schools in the United Kingdom (Oxford, Cambridge, Glasgow, Southampton). After completing his medical qualification and an M.D. in Biochemistry (Münster), Matthias carried out postdoctoral research at the National Institutes of Health (Bethesda, Maryland, USA), before joining EMBL Heidelberg as a Group Leader in 1989. He obtained the Habilitation from Heidelberg University in 1990 and became Professor for Molecular Medicine in 2005. Matthias served as the Dean of Graduate Studies from 1996 until being promoted to the position as EMBL Associate Director in July 2005. In 2013 he was appointed as EMBL Director. As a research scientist, Matthias Hentze has made multiple landmark contributions to the understanding of posttranscriptional gene regulation, especially the control of protein synthesis. His work has also provided fundamental insights into the molecular mechanisms governing iron homeostasis and diseases of altered iron metabolism. Matthias co-founded the Molecular Medicine Partnership Unit (MMPU) between EMBL and the Medical Faculty of Heidelberg University in 2002, which he co-directs and where he conducts translational research on common diseases of iron metabolism and of altered mRNA metabolism. Recent work by the Hentze group has uncovered hundreds of new RNA-binding proteins, including many metabolic enzymes. Supported by an ERC Advanced Grant, their current work focuses on the elucidation of connections between metabolism and gene regulation.

Research Interest

Previous and current research Important steps in the control of gene expression are executed in the cytoplasm by regulation of mRNAs via RNA-binding proteins (RBPs) and non-coding regulatory RNAs. We are elucidating these regulatory mechanisms, combining ‘reductionist’ biochemical and systems level approaches in mammalian, yeast and Drosophila model systems. We developed the techniques of ‘mRNA interactome capture’ – to define ‘all’ RBPs associated with mRNAs in vivo (Castello et al., 2012) – and ‘RBDmap’ – to identify the RNA-binding domains of previously unknown RBPs (Castello et al., 2016). This work led to the discovery that hundreds of seemingly well characterised cellular proteins also bind RNA (enigmRBPs) (Beckmann et al., 2015). These discoveries offer an ideal starting point for exploration of ‘enigmRBPs’ and ‘REM networks’ (Hentze & Preiss, 2010), which we expect to connect cell metabolism and gene expression in previously unrecognised ways (figure 1).