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Brandt, W.

Publications and source records attributed to Brandt, W..

4 recordsLinked to original sources

Ciliary sensing in tanycytes couples nutrient availability to metabolic regulation

Body homeostasis relies on accurate communication between the brain and the periphery. Disruption of this communication can contribute to disease. Tanycytes are located at the interface of the cerebrospinal fluid (CSF), bloodstream, and hypothalamus, where they sense circulating nutrients and regulate neuroendocrine axes and metabolism. However, the mechanisms by which they sense CSF signals remain largely unclear. Recent evidence that tanycytes possess primary cilia -- key sensory organelles -- led us to hypothesize that tanycytic cilia function as sensory antennae that detect metabolic cues in the CSF. Here, we demonstrate that tanycytic cilia exhibit distinct morphologies across subtypes and physiological states. They respond dynamically to hormonal and nutrient availability; notably, excess oleic acid shortens cilia, promotes lipid droplet accumulation, and reduces Ca{superscript 2} responses to ATP and glucose. Disrupting cilia via knockdown of intraflagellar transport (IFT) genes produced similar defects and impaired autophagy. Finally, selective Ift88 knockout in tanycytes increased body weight and reduced thermogenic activity in female mice. These findings identify tanycytic cilia as key sensors regulating energy balance.

neuroscience↗

Bacterial-type plant ferroxidases tune local phosphate sensing in root development

Fluctuating bioavailability of inorganic phosphate (Pi), often caused by complex Pi-metal interactions, guide root tip growth and root system architecture for maximizing the foraged soil volume. Two interacting genes in Arabidopsis thaliana, PDR2 (P5-type ATPase) and LPR1 (multicopper oxidase), are central to external Pi monitoring by root tips, which is modified by iron (Fe) co-occurrence. Upon Pi deficiency, the PDR2-LPR1 module facilitates cell type-specific Fe accumulation and cell wall modifications in root meristems, inhibiting intercellular communication and thus root growth. LPR1 executes local Pi sensing, whereas PDR2 restricts LPR1 function. We show that native LPR1 displays specific ferroxidase activity and requires a conserved acidic triad motif for high-affinity Fe2+ binding and root growth inhibition under limiting Pi. Our data indicate that substrate availability tunes LPR1 function and implicate PDR2 in maintaining Fe homeostasis. LPR1 represents the prototype of an ancient ferroxidase family, which evolved very early upon bacterial colonization of land. During plant terrestrialization, horizontal gene transfer transmitted LPR1-type ferroxidase from soil bacteria to the common ancestor of Zygnematophyceae algae and embryophytes, a hypothesis supported by homology modeling, phylogenomics, and activity assays of bacterial LPR1-type multicopper oxidases.

plant biology↗

Two novel 7-epi-zingiberene derivatives with biological activity from Solanum habrochaites are produced by a single cytochrome P450 monooxygenase

Secretions from glandular trichomes potentially protect the plant against a variety of aggressors. In the tomato genus, wild species constitute a rich source of chemical diversity produced at the leaf surface by glandular trichomes. Previously, 7-epi-zingiberene produced in several accessions of Solanum habrochaites was found to confer resistance to whiteflies (Bemisia tabaci) and other insect pests. Here, we identify two derivatives of 7-epi-zingiberene from S. habrochaites that had not been reported as yet. We identified them as 9-hydroxy-zingiberene and 9-hydroxy-10,11-epoxyzingiberene. Using a combination of genetics and transcriptomics we identified a single cytochrome P450 oxygenase, ShCYP71D184 that carries out two successive oxidations to generate the two sesquiterpenoids. Bioactivity assays showed that only 9-hydroxy-10,11-epoxyzingiberene exhibits substantial toxicity against B. tabaci. In addition, both 9-hydroxy-zingiberene and 9-hydroxy-10,11-epoxyzingiberene display substantial growth inhibitory activities against a range of microorganisms, including Bacillus subtilis, Phytophtora infestans and Botrytis cinerea. Our work shows that trichome secretions from wild tomato species can provide protection against a wide variety of organisms. In addition, the availability of the genes encoding the enzymes for the pathway of 7-epi-zingiberene derivatives makes it possible to introduce this trait in cultivated tomato by precision breeding.

plant biology↗

A cytochrome P450 from juvenile mustard leaf beetles hydroxylates geraniol, a key step in iridoid biosynthesis

Juveniles of the leaf beetle Phaedon cochleariae synthesize iridoid via the mevalonate pathway to repel predators. The normal terpenoid biosynthesis is integrated into the dedicated defensive pathway by the {omega}-hydroxylation of geraniol to 8-hydroxygeraniol. Here we identify and characterize the geraniol 8-hydroxylase as a P450 monooxygenase using integrated transcriptomic and proteomic analyses. In the fat body, 73 individual cytochrome P450s were identified. The double stranded RNA (dsRNA)-mediated knock down of CYP6BH5 led to a significant reduction of 8-hydroxygeraniol-glucoside in the hemolymph and, later, of the chrysomelidial in the defensive secretion. Heterologously expressed CYP6BH5 converted geraniol to 8-hydroxygeraniol. In addition to geraniol, CYP6BH5 also catalyzes other monoterpenols, such as nerol and citronellol, into the corresponding , {omega}-dihydroxy compounds.\n\nHighlightsO_LIThe geraniol 8-hydroxylase in Phaedon cochleariae was identified as a cytochrome P450 CYP6BH5.\nC_LIO_LIRNA interference emphasized the importance of CYP6BH5 in iridoid biosynthesis.\nC_LIO_LIIn vitro enzyme assays showed that recombinant CYP6BH5 is a substrate promiscuous enzyme, converting the {omega}-hydroxylation of geraniol, nerol, citronellol but not linalool.\nC_LIO_LIHomology modeling suggested the -OH group of the substrate plays an important role in coordinating the substrates with the enzymes catalytic cavity.\nC_LI

biochemistry↗