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Molecular Neuroscience Group


Introduction to the Molecular Neuroscience Group


The Molecular Neuroscience Group focuses on investigating the molecular mechanisms that can cause Alzheimer’s disease (AD) and other neurodegenerative diseases, such as Parkinson’s disease (PD) and Huntington’s disease (HD).

A microfluidic-engineered cell culture chamber allows us to monitor separately “donor neurons”, axons and “acceptor neurons” in our study of Tau misfolded state propagation from cell to cell.

Proteins attain their function by folding into 3 dimensional shapes in cells; only if they assume their correct shape can they perform correctly and adopt essential roles that support life. AD, like other neurodegenerative diseases, is caused by aberrant forms of proteins which tend to accumulate and aggregate into shapes, which are believed to be toxic to the brain cells of affected patients. The two proteins thought to cause AD are Amyloid-β (Aβ) and Tau and are part of a group of proteins called amyloid proteins. Amyloids are special in that, under circumstances not yet fully understood, they can ‘misfold’ and in the ensuing misfolded states they have a tendency to clump together and form clusters which accumulate in the brains of patients suffering from AD (and related diseases, such as Parkinson’s and Huntington’s). 

We and others have recently shown that amyloid proteins can travel into and out of cells and also between different compartments within a cell. This so called ‘trafficking’ behaviour has major ramifications for the progression of disease. Trafficking of amyloid proteins between cells may lead to the transmission of their toxicity from one cell to another and thus to spreading the disease to healthy brain tissue. 

Tau (red), a protein involved in Alzheimer’s disease, co-localises with vesicular markers (green), informing us on the fate of Tau after internalisation by primary neurons in culture. The typical size of a vesicle is indicated by the white dashed lines. Scale bar: 500nm.

In order to study these processes in live cells/organisms we use primary neuronal cultures, neuronal cell lines, and small organisms such as the earthworm C. elegans as models of disease. We closely work with Prof. Tuomas Knowles and Dr. Florian Hollfelder on the design of microfluidic devices to study amyloid trafficking across neuronal cells. For superresolution imaging of cells and worms we make use of the Laser Analytics Group’s facility, headed by Prof. Kaminski. We further collaborate closely with Prof. St George Hyslop’s headed Neuroscience Consortium involving expert scientists from the UK and abroad, such as Prof. Dobson in Chemistry, Profs. Mandelkow. On the study of protein trafficking related to neurodegenerative diseases we closely collaborate with Profs. Jucker in Germany and Bates in London.



Parkinson's disease protein plays vital 'marshalling' role in healthy brains

Work in the group has led to the estabilshment of how a protein called alpha-synuclein, which is closely associated with Parkinson's Disease, functions in healthy human brains. By showing how the protein works in healthy patients, the study offers important clues about what may be happening when people develop the disease itself. Read the news article here, or the paper DOI: 10.1038/NCOMMS12563.

Lodged in Late Endosomes, Presenilin 2 Churns Out Intraneuronal Aβ

Read more here.

Jane Fojas awarded a Schlumberger Fellowship

Jane Fojas, a first year PhD student has been awarded a Schlumberger Fellowship. Congratulations Jane!

Researchers identify when Parkinson’s proteins become toxic to brain cells

Research in the group has observed the point at which proteins associated with Parkinson’s disease become toxic to brain cells could help identify how and why people develop the disease, and aid in the search for potential treatments. Read more here.

Protein transfer and structure-specific fluorescence in hydrogen bond-rich protein structures

D Pinotsi, L Grisanti, P Mahou, R Gebauer, CF Kaminksi, AA Hassanali and GS Kaminski Schierle, "Protein transfer and structure-specific fluorescence in hydrogen bond-rich protein structures", J. Am. Chem. Soc. (2016). doi:10.1021/jacs.5b11012