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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
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While the differential rate law relates the rate and concentrations of reactants, a second form of rate law called the integrated rate law relates concentrations of reactants and time. Integrated rate laws can be used to determine the amount of reactant or product present after a period of time or to estimate the time required for a reaction to proceed to a certain extent. For example, an integrated rate law helps determine the length of time a radioactive material must be stored for its...
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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Updated: Jan 22, 2026

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

Mariana E G de Araujo1, Sascha J Amann2,3, Taras Stasyk1

  • 1Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck 6020, Austria.

Proceedings of the National Academy of Sciences of the United States of America
|January 20, 2026
PubMed
Summary

The study reveals the octameric structure of BORC and demonstrates that BORC and BLOC-1 can form hybrid complexes, challenging their distinct roles in endolysosomal trafficking and suggesting dynamic assembly for cellular functions.

Keywords:
BLOC-1BORCEARPlysosomerecycling endosome

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • BORC and BLOC-1 are multisubunit complexes involved in endolysosomal trafficking.
  • Their paralogous origins and shared subunits hint at potential interactions or higher-order assembly.

Purpose of the Study:

  • To elucidate the structural architecture of BORC.
  • To investigate the potential for hybrid complex formation between BORC and BLOC-1.
  • To understand the regulation and functional implications of these complexes in cellular trafficking.

Main Methods:

  • Determined the conserved octameric architecture of BORC using structural biology techniques.
  • Employed cross-linking mass spectrometry to validate the BORC model in human cells.
  • Performed biochemical and structural analyses to identify and characterize BORC-BLOC-1 hybrid complexes.

Main Results:

  • Revealed the conserved octameric structure of BORC, composed of two intertwined tetramers.
  • Validated the BORC structure in human complexes and identified key residues for integrity and lysosomal transport.
  • Provided evidence for BORC-BLOC-1 hybrid complexes, linking them to transferrin receptor recycling via the EARP complex.

Conclusions:

  • BORC and BLOC-1 are not distinct entities but can form dynamic hybrid complexes.
  • Modular assembly of these complexes allows for functional specialization in endolysosomal trafficking.
  • Understanding these complexes offers insights into disease mechanisms and cellular regulation.