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Brumm, S.

Publications and source records attributed to Brumm, S..

2 recordsLinked to original sources

Arabidopsis AZG2, an auxin induced putative cytokinin transporter, regulates lateral root emergence

The phytohormones cytokinin (CK) and auxin are key regulators of plant growth and development. During the last decade specialised transport mechanisms turned out to be the key for the control of local and long distance hormone distributions. In contrast to auxin, CK transport is poorly understood. Here we show that Arabidopsis thaliana AZG2, a member of the AZG purine transporter family, acts as CK transporter involved in the determination of the root system architecture. The expression of AtAZG2 is primarily auxin dependent and restricted to a small group of cells surrounding the lateral root primordia. Compared to wild type, mutants carrying loss-of-function alleles of Atazg2 have higher density of lateral roots, suggesting AZG2 as being part of a regulatory pathway in lateral root emergence. Moreover, azg2 mutants are partially insensitive to exogenously applied CK, which is consistent with the observation that the CK reporter gene TCSnpro:GFP showed lower fluorescence signal in the roots of azg2 mutants compared to those of wild type. These results indicate a defective CK signalling pathway in the region of lateral root primordia. By the integration of AtAZG2 subcellular localization and CK transport capacity data, our results allowed us to propose a local Auxin/CK signalling model for the regulation of lateral root emergence.

plant biology

ARF1 dimerization is essential for vesicle trafficking and dependent on activation by ARF-GEF dimers in Arabidopsis

Membrane traffic maintains the organization of the eukaryotic cell and delivers cargo proteins to their subcellular destinations such as sites of action or degradation. Membrane vesicle formation requires ARF GTPase activation by the SEC7 domain of ARF guanine-nucleotide exchange factors (ARF-GEFs), resulting in the recruitment of coat proteins by GTP-bound ARFs. In vitro exchange assays were done with monomeric proteins, although ARF-GEFs have been shown to form dimers in vivo. This feature is conserved across the eukaryotes, however its biological significance is unknown. Here we demonstrate ARF1 dimerization in vivo and we show that ARF-GEF dimers mediate ARF1 dimer formation. Mutational disruption of ARF1 dimers interfered with ARF1-dependent trafficking but not coat protein recruitment in Arabidopsis. Mutations disrupting simultaneous binding of two ARF1*GDPs by the two SEC7 domains of GNOM ARF-GEF dimer prevented stable interaction of ARF1 with ARF-GEF and thus, efficient ARF1 activation. Our results suggest a model of activation-dependent dimerization of membrane-inserted ARF1*GTP molecules required for coated membrane vesicle formation. Considering the evolutionary conservation of ARFs and ARF-GEFs, this initial regulatory step of membrane trafficking might well occur in eukaryotes in general.

plant biology