Carsten Janke, Institut Curie - 'How the tubulin code controls microtubule functions'
2:00pm - 3:00pm /
Monday 19th January 2026
/ Venue: Physiology seminar room Nuffield Wing
Type: Seminar /
Category: Research
/ Series: Institute of Systems, Molecular and Integrative Biology
- Igor Barsukov
- Admission: Free, no registration required.
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Carsten Janke Janke holds a degree in Biochemistry from the University of Leipzig, where he also performed his PhD with Thomas Arendt. He then worked with Elmar Schiebel at the Beatson Institute for Cancer Research in Glasgow, after which he then moved to the CRBM in Montpellier to work on the tubulin code as a researcher with Bernard Eddé. Since 2005, Carsten heads an independent team, which moved to the Institut Curie in 2010.
Carsten discovered key enzymes involved in tubulin posttranslational modifications and initiated the functional exploration of the tubulin code. He was elected EMBO member in 2014 and coordinates an ERC synergy grant since 2022. Carsten’s current work focusses on the function of the tubulin code from the single molecule to the whole organism.
How the tubulin code controls microtubule functions:
How can microtubules adapt to a broad range of functions in cells? In the 1970s it was proposed that biochemical modulation of tubulin proteins could generate microtubules with specific functions. At about the same time the first posttranslational modifications of tubulin were discovered, providing a potential mechanism to generate this diversity. However, the enzymes catalysing tubulin modifications were mostly discovered 30 years later, explaining why most functional work on the tubulin code has only recently been performed. Somewhat surprisingly, knockout of many of the tubulin-modifying enzymes did not lead to strong phenotypes in cells, but rather to subtle alterations that only become visible as defects in the context of an entire organism, and often get more pronounced during ageing.
Dissection of the molecular mechanisms controlled by tubulin modifications now provides potential clues why this is the case. For many microtubule-associated proteins (MAPs) that can sense tubulin modifications, the modifications tune the affinities rather than being essential for, or preventing, their binding. Thus, the concept of the tubulin code should be seen as a gradual modulation of microtubule-based processes rather than binary switches between different microtubule functions. While such subtle changes are more difficult to observe at the cellular level, their impacts at the organism- and lifetime-scales bear the potential of being essential regulators of physiological processes, and consequently, whose dysregulation can cause disease. Uncovering the molecular basis of the tubulin code can thus lead to the discovery of unsuspected disease mechanisms, thereby opening the door for potential treatment strategies.
All welcome.
Carsten discovered key enzymes involved in tubulin posttranslational modifications and initiated the functional exploration of the tubulin code. He was elected EMBO member in 2014 and coordinates an ERC synergy grant since 2022. Carsten’s current work focusses on the function of the tubulin code from the single molecule to the whole organism.
How the tubulin code controls microtubule functions:
How can microtubules adapt to a broad range of functions in cells? In the 1970s it was proposed that biochemical modulation of tubulin proteins could generate microtubules with specific functions. At about the same time the first posttranslational modifications of tubulin were discovered, providing a potential mechanism to generate this diversity. However, the enzymes catalysing tubulin modifications were mostly discovered 30 years later, explaining why most functional work on the tubulin code has only recently been performed. Somewhat surprisingly, knockout of many of the tubulin-modifying enzymes did not lead to strong phenotypes in cells, but rather to subtle alterations that only become visible as defects in the context of an entire organism, and often get more pronounced during ageing.
Dissection of the molecular mechanisms controlled by tubulin modifications now provides potential clues why this is the case. For many microtubule-associated proteins (MAPs) that can sense tubulin modifications, the modifications tune the affinities rather than being essential for, or preventing, their binding. Thus, the concept of the tubulin code should be seen as a gradual modulation of microtubule-based processes rather than binary switches between different microtubule functions. While such subtle changes are more difficult to observe at the cellular level, their impacts at the organism- and lifetime-scales bear the potential of being essential regulators of physiological processes, and consequently, whose dysregulation can cause disease. Uncovering the molecular basis of the tubulin code can thus lead to the discovery of unsuspected disease mechanisms, thereby opening the door for potential treatment strategies.
All welcome.