Physics-Biology interface seminar

Held every second Wednesday at 11am in the joint seminar room of LPTMS and FAST in Orsay, this seminar series aims to be a central forum for the Physics/Biology interface in the south of Paris.

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Other seminars and conferences you might be interested in:

Paris-Saclay Biomechanics seminar - last Thu. of the month in Palaiseau (subscribe to their announcements)
Seminar of the Physical Chemistry Laboratory - in Orsay

Informations for speakers
Past seminars
Contact the organizer


Heiko Rieger (Saarland University)

Location: Amphi BLANDIN du LPS de la Faculté des Sciences d’Orsay (Bâtiment 510)

Probing proteins in small volumes

Tuomas Knowles (Cambridge University, UK)

Warning: special time

This talk outlines our efforts on exploring experimental strategies to provide a new window into protein self-assembly that are enabled by operation in small volumes. We have shown that microconfinement achieved through droplet microfluidics allows the isolation of single nucleation events in protein aggregation and thus to study a rare event as single molecule resolution. Using this strategy we have also been able to develop an understanding of how aberrant misfolded protein states are transmitted from one molecule to another through time and space. More recently we have exploited measurements of mass transport through fluid streams under laminar flow conditions to generate a platform for probing protein-protein interactions under fully native conditions.

Location: Salle de séminaire LPTMS, bâtiment Pascal n°530

Matthias Merkel (Turing Center for Living Systems, Marseille)

Location: Salle de séminaire LPTMS, bâtiment Pascal n°530

Prion-like propagation of alpha-synuclein assemblies in synucleinopathies, similarities with Tau in Tauopathies

Ronald Melki (Institut François Jacob, CEA & CNRS)

The aggregation of proteins within the central nervous system is deleterious and associated to neurodegenerative disorders. The aggregation of the proteins alpha-synuclein and Tau are associated to synucleinopathies, in particular Parkinson's disease, and tauopathies, among which Alzheimer’s disease, respectively. How alpha-synuclein and Tau aggregates, how those aggregates traffic between cells, amplify by recruiting endogenous monomeric alpha-synuclein or Tau and cause distinct synucleinopathies or tauopathies is unclear. I will explain the molecular events that lead to alpha-synuclein or Tau aggregation. I will show that alpha-synuclein and Tau aggregates bind to neurons cell membranes and explain the cellular consequences of binding. The similarities and differences between alpha-synuclein and Tau will be highlighted. I will explain how alpha-synuclein and Tau aggregates penetrate the cells and get transported. Finally, I will describe how the structure of the fibrillar polymorphs alpha-synuclein and Tau aggregation yield distinct diseases.

References:

  1. Brundin P et al. (2010) Nat Rev Mol Cell Biol. 11:301-7.
  2. Bousset L et al. (2013) Nat Commun. 4:2575.
  3. Peelaerts W et al. (2015) Nature 522:340-4.
  4. Shrivastava AN et al. (2015) EMBO J. 34:2408-23.
  5. Brahic M et al. (2016) Acta Neuropathol. 131:539-48.
  6. Makky A et al. (2016) Sci Rep. 6:37970.
  7. Flavin W et al. (2017) Acta Neuropathol. 134:629-653.
  8. Shrivastava AN et al. (2017) Neuron 95:33-50.
  9. Melki R (2018) Neurobiol Dis. 109:201-208.
  10. Gribaudo S et al. (2019) Stem Cell Reports. 12:230-244.
  11. Shrivastava AN et al. (2019) EMBO J. 38. pii: e99871.
  12. Fenyi A et al., (2019) Neurobiol Dis 129:38-43.
Location: Salle de séminaire LPTMS, bâtiment Pascal n°530

Anne-Virginie Salsac (Université de Technologie de Compiègne)

Location: Salle de séminaire LPTMS, bâtiment Pascal n°530