The LMB congratulates Michel Goedert, who this year has reached the milestone of forty years working at the LMB.
Michel joined the LMB as a postdoctoral scientist in the Director’s Section (renamed Genome Studies in 1991), after receiving an MD from the University of Basel, Switzerland, and a PhD in Pharmacology from the University of Cambridge. He became a Group Leader at the LMB in 1988. Following closure of the Genome Studies Section, Michel joined the Neurobiology Division in 1995. He served as Head of Neurobiology, solely or jointly, from 2003 until 2016.
Throughout his forty years at the LMB, Michel has dedicated his research to a better understanding of Alzheimer’s and other neurodegenerative diseases, resulting in several significant breakthroughs. In 1987, Michel began working with Aaron Klug, Tony Crowther, Claude Wischik and John Walker to decipher the molecular nature of the paired helical and straight filaments of Alzheimer’s disease. By 1988 the group had shown that tau protein is an integral component of these filaments. This work also led to identification of the tau isoforms that are expressed in central and peripheral nervous systems. In 1998, Michel and his collaborators showed that inherited mutations in the tau gene can cause a form of dementia that is accompanied by abundant filamentous tau inclusions, establishing that the dysfunction of tau protein is sufficient to cause neurodegeneration and dementia. The assembly of tau into amyloid filaments and their prion-like propagation through the brain are characteristic of a number of neurodegenerative diseases.
In 1997, working with Maria Grazia Spillantini and Ross Jakes, Michel identified alpha-synuclein as the major component of Lewy bodies and Lewy neurites, which are the defining neuropathological characteristics of Parkinson’s disease and dementia with Lewy bodies. In 1998, he identified multiple system atrophy as the third major synucleinopathy.
Since 2017, Michel has worked closely with Sjors Scheres from the LMB’s Structural Studies Division. Together, their groups have shown that tau and alpha-synuclein amyloid filaments extracted from human brains can adopt distinct structures in different diseases, opening up the possibility to study the underlying mechanisms.