Dr. Rachel Curnock
My research involves understanding how endosomal sorting complexes are regulated at the transcriptional and post-transcriptional level.
I am particularly interested in identifying upstream regulatory proteins and upstream stimuli that modulate the stability and function of the retromer and WASH complexes.
I am also interested in furthering our understanding of the role of the retromer complex in lysosomal health and the homeostasis of nutrient-sensing receptors.
Prof. Pete Cullen
I did my PhD with Alan Dawson in Norwich. I tried to define the role of inositol phosphates in the regulation of receptor-mediated calcium homeostasis. I also began to develop the appreciation that to understand a complex process you must have a strong underlying molecular foundation.
So, I then did a post-doc with Robin Irvine in Cambridge. Here, I learned about protein purification and molecular cloning in an environment where I also learned how to be a research scientist.
In starting my own laboratory in Bristol, we initially continued to examine the role of phosphoinositides in receptor signalling. In 2002, we chose to re-focus our research into trying to define the role phosphoinositides in orchestrating the sorting of integral membrane proteins through the endosomal network.
Our strength now is to combine the molecular identification of multi-protein endosomal sorting complexes with their quantitative functional analysis in vitro and more recently in vivo in the context of Drosophila development and physiology.
I am studying how the SNX-BAR proteins, members of the sorting nexin family, associate with endosomal membrane to coordinate the formation of discrete tubular profiles and tubulovesicular transport carriers that are essential for cargo recycling.
In particular I am interested in understanding how the spatially and biochemically diverse SNX-BAR complexes couple the selection of cargo to the biogenesis of endosome-derived transport carriers.
I have extensively used quantitative proteomics to obtain a comprehensive list of SNX-BAR proteins inetractors and I have been developing proteomics tools to further investigate endosome recycling.
I research the SNX3-retromer complex and the mechanisms behind its retrieval of Wntless, a chaperone indispensable for the secretion of Wnt morphogens.
I am also interested retromer's role in neurodegeneration, particularly Parkinson's disease.
I'm Kerrie and I'm a final year PhD student in Pete's lab.
I'm interested in the mechanisms of retromer-independent retrieval and recycling of cargo.
I hope to complement my in vitro knowledge of endosomal sorting with in vivo analysis in Drosophila.
My research focuses upon an evolutionarily conserved family of proteins classified by the presence of a Phox-homology (PX) domain, the Sorting nexins (SNXs).
As the modular SNX PX domain constitutes a phosphoinositide binding motif, SNXs localise to and function from endosomal compartments in which these lipids are enriched.
I am particularly interested in how the defining PX domain is combined with other functional modules to confer diverse roles to the SNX family in the co-ordination of endosomal sorting and signalling and how perturbations to their function relate to a variety of diseases.
Dr. Chris Danson
Dr. Paul Langton
I am studying the in vivo role of two recently identified endosomal sorting complexes, the Retriever and CCC complexes, using Drosophila melanogaster as a model organism.
I am using CRIPSR/Cas9 to generate knock-outs and tag endogenous proteins, and will use these tools to study the role of these complexes during development and adult homeostasis.
Dr. Neil Pearson
I introduced Drosophila to the lab when I joined in 2012.
Since then I've been generating mutants to gain insights into the in vivo function of various sorting nexins in the fly.
I'm currently dissecting the roles of SNX27 and SNX20 with a focus on Drosophila development.
My research is focused on investigating the role of the endosomal network in neurological disorders.
In particular I am interested in understanding how disruption of the retromer complex is involved in the pathology of Parkinson's disease