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TitleBORC assemblies integrate BLOC-1 subunits to diversify endosomal trafficking functions.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 4, Page e2515691123, Year 2026
Publish dateJan 27, 2026
AuthorsMariana E G de Araujo / Sascha J Amann / Taras Stasyk / Alexander Schleiffer / Eva Rauch / Paula Flümann / Isabel I 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 / Lukas A Huber /
PubMed AbstractBORC and BLOC-1 are multisubunit complexes that regulate endolysosomal trafficking. Although they are presumed to be distinct, their paralogous origins and shared subunits suggest the potential for ...BORC and BLOC-1 are multisubunit complexes that regulate endolysosomal trafficking. Although they are presumed to be distinct, their paralogous origins and shared subunits suggest the potential for higher-order assembly. Here, we reveal the conserved octameric architecture of BORC formed by two intertwined tetramers and present the structure of C. elegans BORC. Through cross-linking mass spectrometry of endogenous complexes, we validate this model for human BORC and demonstrate that the integrity of the complex, which is essential for lysosomal transport, relies on specific interfacial residues. We also clarify the disruptive nature of disease-causing mutations and propose that the formation and function of BORC are likely regulated by specific cues. These cues might include the phosphorylation of Snapin and a pH-sensitive histidine residue in BORCS5. Additionally, we present direct biochemical and structural evidence of BORC-BLOC-1 hybrid complexes. Finally, we link a specific hybrid complex to the regulation of transferrin receptor recycling via interaction with the EARP complex. Our work challenges the paradigm of BORC and BLOC-1 as separate entities, establishing a model of dynamic complex formation wherein modular assembly creates functional specialization to meet diverse cellular demands.
External linksProc Natl Acad Sci U S A / PubMed:41557793 / PubMed Central
MethodsEM (single particle)
Resolution7.8 Å
Structure data

56129

9tqb

EMDB-56129, PDB-9tqb:
Octameric C. elegans BORC, containing BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and the shared BORC and BLoC-1 subunits, BLOC1S1, BLOC1S2 and Snapin
Method: EM (single particle) / Resolution: 7.8 Å

Source
  • caenorhabditis elegans (invertebrata)
  • caenorhabditis (invertebrata)
KeywordsTRANSPORT PROTEIN / BORC / BLOC-1 / lysosome / recycling endosome / EARP

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