H(+) V-ATPases (V-ATPases) are found in two principal locations, in endomembranes and in plasma membranes. The plasma membrane V-ATPase from the midgut of larval Manduca sexta is the sole energizer of all transepithelial secondary transport processes. At least two properties make the lepidopteran midgut a model tissue for studies of general aspects of V-ATPases. First, it is a rich source for purification of the enzyme and therefore for structural studies: 20 larvae provide up to 0.5 mg of holoenzyme, and soluble, cytosolic V(1) complexes can be obtained in even greater amounts of up to 2 mg. Second, midgut ion-tranport processes are strictly controlled by the regulation of the V-ATPase, which is the sole energizer of all ion transport in this epithelium. Recent advances in our understanding the structure of the V(1) and V(o) complexes and of the regulation of the enzyme's biosynthesis and ion-transport activity will be discussed.
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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