Membrane extraction by calmodulin underpins the disparate signalling of RalA and RalB.
View / Open Files
Publication Date
2022-06Journal Title
Bioessays
ISSN
0265-9247
Publisher
Wiley
Type
Article
This Version
AM
Metadata
Show full item recordCitation
Chamberlain, S. G., Owen, D., & Mott, H. R. (2022). Membrane extraction by calmodulin underpins the disparate signalling of RalA and RalB.. Bioessays https://doi.org/10.1002/bies.202200011
Abstract
Both RalA and RalB interact with the ubiquitous calcium sensor, calmodulin (CaM). New structural and biophysical characterisation of these interactions strongly suggests that, in the native membrane-associated state, only RalA can be extracted from the membrane by CaM and this non-canonical interaction could underpin the divergent signalling roles of these closely related GTPases. The isoform specificity for RalA exhibited by CaM is hypothesised to contribute to the disparate signalling roles of RalA and RalB in mitochondrial dynamics. This would lead to CaM shuttling RalA to the mitochondrial membrane but leaving RalB localisation unperturbed, and in doing so triggering mitochondrial fission pathways rather than mitophagy.
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/E013228/1)
BBSRC (BB/P504835/1)
Embargo Lift Date
2023-03-23
Identifiers
External DOI: https://doi.org/10.1002/bies.202200011
This record's URL: https://www.repository.cam.ac.uk/handle/1810/334909
Statistics
Total file downloads (since January 2020). For more information on metrics see the
IRUS guide.