From one complex to many: Rethinking the BLOC/BORC system

Two protein complexes that regulate intracellular transport and lysosome positioning were long thought to exist as single, well-defined entities. New structural insights now come from the groups of David Haselbach and Tim Clausen of the Research Institute of Molecular Pathology (IMP) and a collaboration with former IMP group leader Lukas Huber - now at the Medical University Innsbruck. Their study, published in the journal PNAS, redefines BLOC-1 and BORC as families of related complexes, providing a foundation to study their functions more accurately.

Architecture of the BORC complex, based on a cryo-electron microscopy density map with fitted molecular models. Click to enlarge.

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Original publication

Mariana E.G. de Araujo, Sascha Amann, Taras Stasyk, Alexander Schleiffer, Eva Rauch, Paula Flümann, Isabel Singer, Leopold Kremser, Vojtech Dostal, Thanida Laopanupong, Nikolaus Obojes, Moritz H. Wallnöfer, Flora S. Gradl, Robert Kurzbauer, Caroline Krebiehl, Samuel Kofler, Irina Grishkovskaya, Georg F. Vogel, Michael W. Hess, Bettina Sarg, Tim Clausen; David Haselbach and Lukas A. Huber (2026): "BORC assemblies integrate BLOC-1 subunits to diversify endosomal trafficking functions". PNAS (2026). DOI: 10.1073/pnas.2515691123

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