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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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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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The endosymbiont theory is the most widely accepted theory of eukaryotic evolution; however, its progression is still somewhat debated. According to the nucleus-first hypothesis, the ancestral prokaryote first evolved a membrane to enclose DNA and form the nucleus. Conversely, the mitochondria-first hypothesis suggests that the nucleus was formed after endosymbiosis of mitochondria.
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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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Diversity, Origin and Evolution of the ESCRT Systems.

Kira S Makarova1, Victor Tobiasson1, Yuri I Wolf1

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The Endosomal Sorting Complexes Required for Transport (ESCRT) system likely originated in the Last Archaeal Common Ancestor, with complex versions evolving in Asgardarchaeota and simpler forms in other archaea. This system predates eukaryotes and bacteria.

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Area of Science:

  • Cell Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Endosomal Sorting Complexes Required for Transport (ESCRT) are crucial for protein sorting in eukaryotes.
  • ESCRT homologs are found in archaea, particularly Asgardarchaeota, the closest archaeal relatives to eukaryotes.
  • Bacteria lack identifiable ESCRT components.

Purpose of the Study:

  • To comprehensively search for ESCRT protein homologs across archaea.
  • To reconstruct the evolutionary history of ESCRT systems.
  • To investigate the origins of eukaryotic ESCRT complexes.

Main Methods:

  • Sensitive protein sequence analysis.
  • Comparison of structural models.
  • Phylogenetic analysis using Vps4 ATPase (ESCRT IV) as a scaffold.

Main Results:

  • Identified diverse ESCRT systems in archaea outside Asgard, including proteins similar to eukaryotic ESCRT-I and ESCRT-II.
  • Found distant CdvA homologs in Thermoproteales, suggesting a role in cell division.
  • Revealed that Asgardarchaeota possess ESCRT complexes linked to the ubiquitin system, a trait previously thought unique to eukaryotes.

Conclusions:

  • The Last Archaeal Common Ancestor likely had a complex ESCRT system for protein sorting.
  • Eukaryotic ESCRT likely evolved from ancestral archaeal building blocks.
  • ESCRT evolution in archaea involved simplification (e.g., TACK) or complexification (e.g., Asgardarchaeota).