Publications by authors named "J D Bangs"

Unlabelled: The protozoan parasite is the only known eukaryote capable of synthesizing the three main phosphosphingolipids: sphingomyelin (SM), inositol phosphorylceramide (IPC), and ethanolamine phosphorylceramide (EPC). It has four paralogous genes encoding sphingolipid synthases (). TbSLS1 is a dedicated IPC synthase, TbSLS2 is a dedicated EPC synthase, and TbSLS3 and TbSLS4 are bifunctional SM/EPC synthases.

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Secretory cargos are exported from the ER via COPII coated vesicles that have an inner matrix of Sec23/Sec24 heterotetramers and an outer cage of Sec13/Sec31 heterotetramers. In addition to COPII, Sec13 is part of the nuclear pore complex (NPC) and the regulatory SEA/GATOR complex in eukaryotes, which typically have one Sec13 orthologue. The kinetoplastid parasite has two paralogues: TbSec13.

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Phosphosphingolipids (PSL) are essential components of eukaryotic membranes. The major PSL in fungi and protists is inositol phosphorylceramide (IPC), while sphingomyelin (SM), and to a lesser extent ethanolamine phosphorylceramide (EPC) predominate in mammals. Most kinetoplastid protozoa have a syntenic locus that encodes a single sphingolipid synthase (SLS) gene.

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Article Synopsis
  • Eukaryotic cells have a secretory pathway that facilitates the transport of proteins between cellular compartments, particularly from the endoplasmic reticulum to the Golgi apparatus via COPII vesicles.
  • In African trypanosomes, two forms of the proteins Sec23 and Sec24 form necessary complexes for transporting specific proteins, like GPI-anchored proteins (GPI-APs), which differ in function between their bloodstream form (BSF) and procyclic form (PCF).
  • Research indicates that these proteins are essential for maintaining protein trafficking processes across different life stages of the trypanosomes, revealing adaptations that optimize their secretory pathways for varying environments.
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African trypanosomes evade the immune system of the mammalian host by the antigenic variation of the predominant glycosylphosphatidylinositol (GPI)-anchored surface protein, variant surface glycoprotein (VSG). VSG is a very stable protein that is turned over from the cell surface with a long half-life (~26 h), allowing newly synthesized VSG to populate the surface. We have recently demonstrated that VSG turnover under normal growth is mediated by a combination of GPI hydrolysis and direct shedding with intact GPI anchors.

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