BORC assemblies integrate BLOC-1 subunits to diversify endosomal trafficking functions

M Mariana E. G. de Araujo (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) S Sascha J. Amann (Research Institute of Molecular Pathology, Vienna BioCenter) T Taras Stasyk (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) A Alexander Schleiffer E Eva Rauch (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) P Paula Flümann (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) I Isabel I. Singer (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) L Leopold Kremser (Institute of Medical Biochemistry, Protein Core Facility, Biocenter, Medical University of Innsbruck) V Vojtech Dostal (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) T Thanida Laopanupong (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) N Nikolaus Obojes (Institute for Alpine Environment, Eurac Research) M Moritz H. Wallnöfer (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) F Flora S. Gradl (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) R Robert Kurzbauer (Research Institute of Molecular Pathology, Vienna BioCenter) C Caroline Krebiehl (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) S Samuel Kofler (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) I Irina Grishkovskaya (Research Institute of Molecular Pathology, Vienna BioCenter) G Georg F. Vogel (Institute of Cell Biology, Biocenter, Medical University of Innsbruck) M Michael W. Hess (Institute of Histology and Embryology, Medical University of Innsbruck) B Bettina Sarg (Institute of Medical Biochemistry, Protein Core Facility, Biocenter, Medical University of Innsbruck) T Tim Clausen D David Haselbach (Research Institute of Molecular Pathology, Vienna BioCenter) L Lukas A. Huber (Institute of Cell Biology, Biocenter, Medical University of Innsbruck)

Abstract

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.

Article Details

Volume / Issue Vol. 123, Issue 4
Published January 27, 2026
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (23)

M

Mariana E. G. de Araujo

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

S

Sascha J. Amann

Research Institute of Molecular Pathology, Vienna BioCenter

T

Taras Stasyk

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

A

Alexander Schleiffer

E

Eva Rauch

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

P

Paula Flümann

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

I

Isabel I. Singer

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

L

Leopold Kremser

Institute of Medical Biochemistry, Protein Core Facility, Biocenter, Medical University of Innsbruck

V

Vojtech Dostal

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

T

Thanida Laopanupong

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

N

Nikolaus Obojes

Institute for Alpine Environment, Eurac Research

M

Moritz H. Wallnöfer

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

F

Flora S. Gradl

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

R

Robert Kurzbauer

Research Institute of Molecular Pathology, Vienna BioCenter

C

Caroline Krebiehl

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

S

Samuel Kofler

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

I

Irina Grishkovskaya

Research Institute of Molecular Pathology, Vienna BioCenter

G

Georg F. Vogel

Institute of Cell Biology, Biocenter, Medical University of Innsbruck

M

Michael W. Hess

Institute of Histology and Embryology, Medical University of Innsbruck

B

Bettina Sarg

Institute of Medical Biochemistry, Protein Core Facility, Biocenter, Medical University of Innsbruck

T

Tim Clausen

D

David Haselbach

Research Institute of Molecular Pathology, Vienna BioCenter

L

Lukas A. Huber

Institute of Cell Biology, Biocenter, Medical University of Innsbruck