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Related Concept Videos

Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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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Mitochondrial Protein Sorting01:39

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Translocation of Proteins into the Mitochondria

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Imaging ATG9A, a Multi-Spanning Membrane Protein
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Structural basis of Vta1 function in the multivesicular body sorting pathway.

Junyu Xiao1, Hengchuan Xia, Jiahai Zhou

  • 1Life Sciences Institute and Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor, MI 48109, USA.

Developmental Cell
|January 16, 2008
PubMed
Summary

Vta1 protein regulates the Vps4 ATPase in the multivesicular body (MVB) pathway. Structural analysis reveals how Vta1

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Reconstitution of Msp1 Extraction Activity with Fully Purified Components

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • The multivesicular body (MVB) pathway is crucial for eukaryotic cellular processes.
  • Efficient MVB pathway function depends on the reversible membrane association of ESCRT proteins, regulated by Vps4 ATPase.
  • The precise mechanism by which Vta1 regulates Vps4 activity remained unclear.

Purpose of the Study:

  • To elucidate the regulatory mechanism of Vps4 by Vta1.
  • To determine the high-resolution crystal structures of key Vta1 domains.
  • To understand Vta1's role in coordinating ESCRT-III assembly and disassembly.

Main Methods:

  • X-ray crystallography to determine the structures of Vta1 domains.
  • Biochemical analysis to assess Vta1 dimerization and Vps4 binding.
  • Structural analysis to propose a mechanism of Vps4 regulation.

Main Results:

  • High-resolution crystal structures of the N-terminal (Did2- and Vps60-binding) and C-terminal (Vps4-binding) domains of S. cerevisiae Vta1 were obtained.
  • The Vta1 C-terminal domain mediates dimerization, and both subunits are essential for Vps4 regulation.
  • A regulatory mechanism where Vta1's C-terminal domain stabilizes Vps4 double rings and the N-terminal domain facilitates ESCRT-III interaction was proposed.

Conclusions:

  • Vta1 acts as a crucial regulator of the Vps4 ATPase in the MVB pathway.
  • Vta1's structure enables it to stabilize Vps4 assembly and coordinate ESCRT-III dynamics.
  • This provides new insights into the regulation of membrane trafficking and protein sorting.