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The Arabidopsis V-ATPase is localized to the TGN/EE via a seed plant-specific motif.


ABSTRACT: The V-ATPase is a versatile proton-pump found in a range of endomembrane compartments yet the mechanisms governing its differential targeting remain to be determined. In Arabidopsis, VHA-a1 targets the V-ATPase to the TGN/EE whereas VHA-a2 and VHA-a3 are localized to the tonoplast. We report here that the VHA-a1 targeting domain serves as both an ER-exit and as a TGN/EE-retention motif and is conserved among seed plants. In contrast, Marchantia encodes a single VHA-isoform that localizes to the TGN/EE and the tonoplast in Arabidopsis. Analysis of CRISPR/Cas9 generated null alleles revealed that VHA-a1 has an essential function for male gametophyte development but acts redundantly with the tonoplast isoforms during vegetative growth. We propose that in the absence of VHA-a1, VHA-a3 is partially re-routed to the TGN/EE. Our findings contribute to understanding the evolutionary origin of V-ATPase targeting and provide a striking example that differential localization does not preclude functional redundancy.

SUBMITTER: Lupanga U 

PROVIDER: S-EPMC7717909 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature

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The Arabidopsis V-ATPase is localized to the TGN/EE via a seed plant-specific motif.

Lupanga Upendo U   Röhrich Rachel R   Askani Jana J   Hilmer Stefan S   Kiefer Christiane C   Krebs Melanie M   Kanazawa Takehiko T   Ueda Takashi T   Schumacher Karin K  

eLife 20201125


The V-ATPase is a versatile proton-pump found in a range of endomembrane compartments yet the mechanisms governing its differential targeting remain to be determined. In Arabidopsis, VHA-a1 targets the V-ATPase to the TGN/EE whereas VHA-a2 and VHA-a3 are localized to the tonoplast. We report here that the VHA-a1 targeting domain serves as both an ER-exit and as a TGN/EE-retention motif and is conserved among seed plants. In contrast, Marchantia encodes a single VHA-isoform that localizes to the  ...[more]

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