Cell Signalling Laboratory

 
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COMPARTMENTALISATION

The cell consists of discrete compartments (organelles) such as the nucleus, Golgi, endoplasmic reticulum, plasma membrane, endosomes and mitochondria that are separated from each other by a protein rich soup called cytosol. Each organelle specialises in a different function by concentrating different groups of proteins and lipids together and regulating their interactions.

Ras proteins are found on most organelles but are particularly concentrated on the cell surface where the upstream receptors that activate them are localised. Whilst superficially all four of the Ras isoforms appear to have similar distributions there are two main areas of difference:

1. The cell surface consists of a mosaic of microdomains that cluster different pools of proteins and lipids into tiny (<20 nanometer) patches visible only using electron microscopy or advanced light microscopy techniques. The different Ras isoforms do not appear to co-localise in these patches; a model that we are testing is that these different Ras microdomains will have different pools of signalling proteins preferentially co-localised allowing each type of microdomain to generate a different output.

2. Ras isoforms are found on internal organelles to different extents. For example, N-Ras is often more strongly associated with the Golgi complex (bright central spot in images below) than the other isoforms. This means that it is likely to be better at activating pathways localised on this organelle than the other isoforms.



 

Latest news
PhD and Post-doc opportunities available, contact me for details

Group members
Veronica Aran, Alison Beckett, Maria Hernandez-Valladares, Craig Mageean, Anna Newlaczyl

Key collaborators
I share lab space and several projects with Mike Clague, Sylvie Urbe and Judy Coulson.

Productive long term interactions exist with the Royle lab investigating mitotic spindle assembly and with the Brust lab developing novel biofunctionalised nano materials.


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