ArticleDevelopment (Cambridge, England)2016
Role of the ABC transporter Mdr49 in Hedgehog signaling and germ cell migration.
Article in Development (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Genotoxicity of Artificial Sweetener Combinations: An Integrated Drosophila melanogaster SMART Assay and Computational Modeling Approach.Molecular genetics and genomics : MGG · 2026Article
- Hedgehog and Drosophila germ cell migration.Development (Cambridge, England) · 2025Review
- Solute carrier (SLC) expression reveals skeletogenic cell diversity.Developmental biology · 2023Article
- Hedgehog signaling guides migration of primordial germ cells to the Drosophila somatic gonad.Genetics · 2023Article
- Germline stem cells in human.Signal transduction and targeted therapy · 2022Review
- Dissection of the microRNA Network Regulating Hedgehog Signaling inFrontiers in cell and developmental biology · 2022Article
- Early patterning of ABCB, ABCC, and ABCG transporters establishes unique territories of small molecule transport in embryonic mesoderm and endoderm.Developmental biology · 2021Article
- Hedgehog signaling and Tre1 regulate actin dynamics through PI(4,5)PCell reports · 2021Article
- Functional analysis of Niemann-Pick disease type C family protein, NPC1a, inDevelopment (Cambridge, England) · 2019Article
- Article
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8 authors.
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Abstract
Coalescence of the embryonic gonad in Drosophila melanogaster requires directed migration of primordial germ cells (PGCs) towards somatic gonadal precursor cells (SGPs). It was recently proposed that the ATP-binding cassette (ABC) transporter Mdr49 functions in the embryonic mesoderm to facilitate the transmission of the PGC attractant from the SGPs; however, the precise molecular identity of the Mdr49-dependent guidance signal remained elusive. Employing the loss- and gain-of-function strategies, we show that Mdr49 is a component of the Hedgehog (hh) pathway and it potentiates the signaling activity. This function is direct because in Mdr49 mutant embryos the Hh ligand is inappropriately sequestered in the hh-expressing cells. Our data also suggest that the role of Mdr49 is to provide cholesterol for the correct processing of the Hh precursor protein. Supporting this conclusion, PGC migration defects in Mdr49 embryos are substantially ameliorated by a cholesterol-rich diet.
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