Publications by authors named "Maria Monastirioti"

Hey is a basic helix-loop-helix-orange (bHLH-O) protein with an important role in the establishment of distinct identities of postmitotic cells. We have previously identified Hey as a transcriptional target and effector of Notch signalling during the asymmetric division of neuronal progenitors, generating neurons of two types, and we have shown that Notch-dependent expression of Hey also marks a subpopulation of the newborn enteroendocrine (EE) cells in the midgut primordium of the embryo. Here, we investigate the transcriptional regulation of in neuronal and intestinal tissues.

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The cytochrome P450 enzymes of the CYP4G subfamily are some of the most intriguing insect P450s in terms of structure and function. In Drosophila, CYP4G1 is highly expressed in the oenocytes and is the last enzyme in the biosynthesis of cuticular hydrocarbons, while CYP4G15 is expressed in the brain and is of unknown function. Both proteins have a CYP4G-specific and characteristic amino acid sequence insertion corresponding to a loop between the G and H helices whose function is unclear.

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Hey is a conserved transcription factor of the bHLH-Orange family that participates in the response to Notch signaling in certain tissues. Whereas three Hey paralogues exist in mammalian genomes, possesses a single gene. Fly Hey is expressed in the subset of newborn neurons that receive a Notch signal to differentiate them from their sibling cells after the asymmetric division of precursors called ganglion-mother-cells.

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The inability of differentiated cells to maintain their identity is a hallmark of age-related diseases. We found that the transcription factor Hey supervises the identity of differentiated enterocytes (ECs) in the adult midgut. Lineage tracing established that Hey-deficient ECs are unable to maintain their unique nuclear organization and identity.

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Enhancer-of-split (E(spl)) was genetically characterized in Drosophila as a dominant mutation that interacts with an allele of Notch, the receptor in a multipurpose signaling pathway throughout development. Although dominant mutations are often not informative of the normal gene function, E(spl) turned out to encode a family of seven paralogous basic helix-loop-helix proteins of utmost importance in the implementation of the Notch signal in the receiving cell. They are transcriptionally induced by Notch in almost every instance where the signal is deployed, and they participate in numerous feedback circuits, where they interface with a panoply of additional more tissue-specific Notch targets to ensure the proper signaling outcome.

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The central complex is a group of modular neuropils in the insect brain with a key role in visual memory, spatial orientation, and motor control. In desert locusts the neurochemical organization of the central complex has been investigated in detail, including the distribution of dopamine-, serotonin-, and histamine-immunoreactive neurons. In the present study we identified neurons immunoreactive with antisera against octopamine, tyramine, and the enzymes required for their synthesis, tyrosine decarboxylase (TDC) and tyramine β-hydroxylase (TBH).

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bHLH-O proteins are a subfamily of the basic-helix-loop-helix transcription factors characterized by an 'Orange' protein-protein interaction domain. Typical members are the Hairy/E(spl), or Hes, proteins, well studied in their ability, among others, to suppress neuronal differentiation in both invertebrates and vertebrates. Hes proteins are often effectors of Notch signalling.

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The catecholamines play a major role in the regulation of behavior. Here we investigate, in the fly Drosophila melanogaster, the role of dopamine and octopamine (the presumed arthropod homolog of norepinephrine) during the formation of appetitive and aversive olfactory memories. We find that for the formation of both types of memories, cAMP signaling is necessary and sufficient within the same subpopulation of mushroom-body intrinsic neurons.

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Octopamine is an important neuroactive substance that modulates several physiological functions and behaviors of invertebrate species. Its biosynthesis involves two steps, one of which is catalyzed by Tyramine beta-hydroxylase enzyme (TBH). The Tbetah gene has been previously cloned from Drosophila melanogaster, and null mutations have been generated resulting in octopamine-less flies that show profound female sterility.

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