Vacuolar-type ATPases (V-ATPases) are proton-translocating enzymes that occur in the endomembranes of all eukaryotes and in the plasma membranes of many eukaryotes. They are multisubunit, heteromeric proteins composed of two structural domains, a peripheral, catalytic V1 domain and a membrane-spanning V0 domain. Both the multitude of locations and the heteromultimeric structure make it likely that the expression and the activity of V-ATPases are regulated in various ways. Regulation of gene expression encompasses control of transcription as well as control at the post-transcriptional level. Regulation of enzyme activity encompasses many diverse mechanisms such as disassembly/reassembly of V1 and V0 domains, oxidation of SH groups, control by activator and inhibitor proteins or by small signalling molecules, and sorting of the holoenzyme or its subunits to target membranes.
Recognising our community as we approach JEB's centenary
In this Editorial, Craig Franklin, Michaela Handel and Kathryn Knight reflect on recent developments at JEB and acknowledge the support of the community during what has been a particularly challenging year. Looking forward, they discuss the journal’s centenary celebrations in 2023.
Our Transformative Journals have exceeded their OA growth targets
In the field: an interview with Roger Hanlon
Roger Hanlon talks about his fieldwork experiences diving all over the planet to understand cephalopod camouflage and communication.
How climbing parrots achieve pitch stability while ascending
Climbing parrots push and pull with their feet on ladder rungs and push with their tails to prevent themselves from toppling backward as they ascend.
Towards understanding the neural origins of hibernation
Madeleine Junkins, Sviatoslav Bagriantsev and Elena Gracheva review the role of the nervous system in hibernation, arguing that it actively promotes and supports the hibernation process rather than simply enduring it.
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