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Inositol pyrophosphates activate the vacuolar transport chaperone complex in yeast by disrupting a homotypic SPX domain interaction

Pipercevic et al resolve how inositol molecules activate the VTC protein complex. The VTC complex stores phosphate in yeast and is controlled by SPX domains. The inositol molecules break an interaction between SPX domains to activate the complex.

Joka Pipercevic
Bastian Kohl
Sebastian Hiller
ResearchOpen Access08 May 2023
Nature Communications

Volume: 14, P: 1-12
Gasdermin-A3 pore formation propagates along variable pathways

Gasdermin-A3 pore formation propagates along diverse pathways. It begins with membrane attachment and oligomeric pre-assembly. Once inserted in the membrane, the oligomers re-assemble into various shapes and sizes, which open their lytic pores.

Stefania A. Mari
Kristyna Pluhackova
Daniel J. Müller
ResearchOpen Access11 May 2022
Nature Communications

Volume: 13, P: 1-14
Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis

Plants regulate phosphate homeostasis via the interaction of PHR transcription factors with SPX receptors bound to inositol pyrophosphate signaling molecules. Here the authors show that inositol pyrophosphate-bound SPX interacts with the coiled-coil domain of PHR, which regulates the oligomerization and activity of the transcription factor.

Martina K. Ried
Rebekka Wild
Michael Hothorn
ResearchOpen Access15 Jan 2021
Nature Communications

Volume: 12, P: 1-13

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Inositol pyrophosphates activate the vacuolar transport chaperone complex in yeast by disrupting a homotypic SPX domain interaction

Gasdermin-A3 pore formation propagates along variable pathways

Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis

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