Explore the words cloud of the NeuroRhomboid project. It provides you a very rough idea of what is the project "NeuroRhomboid" about.
The following table provides information about the project.
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD
|Coordinator Country||United Kingdom [UK]|
|Total cost||183˙454 €|
|EC max contribution||183˙454 € (100%)|
1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
|Duration (year-month-day)||from 2015-04-07 to 2017-04-06|
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|1||THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD||UK (OXFORD)||coordinator||183˙454.00|
Proteases control major pathways in the nervous system and aberrant proteolysis underlies many neurobiological disorders and diseases e.g. Alzheimer's and Parkinson's disease. Signal generation and release is tightly regulated by protease activity, as many key signalling factors are synthesised as transmembrane precursors that require cleavage to liberate their active ectodomains. The largest family of intramembrane proteases are the newly discovered rhomboids, which are found in all kingdoms of life. To date, their physiological significance in mammals is largely unknown, as is the substrate-selectivity of most mammalian rhomboids. I have exciting preliminary data that two uncharacterised mammalian rhomboids, RHBDL1 and RHBDL3, are specifically highly expressed in primary neurons in the CNS. Unlike the well-studied RHBDL2 and Drosophila rhomboids 1-3, they do not have activity against EGF-like growth factors, so they are likely to cleave a novel substrate. A major limitation in protease research has been the lack of unbiased and systematic screens for their substrates. Addressing this deficiency, first, I aim to identify RHBDL1/3-dependent substrates in primary neurons, by adapting recently developed biochemical assays, such as SPECS and BioID. My second aim is the mechanistic validation of these substrates. Third, I will be the first to study the physiological role for active rhomboids, using CRISPR-mediated knock-out neurons and mice. By discovering the role and function of RHBDL1/3 in the brain, I will make an important contribution towards the elucidation of the physiological and medical significance of rhomboid proteases in mammals.
|year||authors and title||journal||last update|
Viorica L. Lastun, Adam G. Grieve, Matthew Freeman
Substrates and physiological functions of secretase rhomboid proteases
published pages: 10-18, ISSN: 1084-9521, DOI: 10.1016/j.semcdb.2016.07.033
|Seminars in Cell & Developmental Biology 60||2019-07-24|
Adam Graham Grieve, Hongmei Xu, Ulrike KÃ¼nzel, Paul Bambrough, Boris Sieber, Matthew Freeman
Phosphorylation of iRhom2 at the plasma membrane controls mammalian TACE-dependent inflammatory and growth factor signalling
published pages: , ISSN: 2050-084X, DOI: 10.7554/eLife.23968
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