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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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Introduction to Membrane Traffic01:44

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The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
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Maturation of Endosomes01:28

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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).
Changes in location
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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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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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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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Related Experiment Video

Updated: Mar 20, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Membrane Tethering Complexes in the Endosomal System.

Anne Spang1

  • 1Biozentrum, Growth & Development, University of Basel Basel, Switzerland.

Frontiers in Cell and Developmental Biology
|June 1, 2016
PubMed
Summary
This summary is machine-generated.

Cellular membrane fusion relies on tethering complexes like CORVET and HOPS. This review explores known and potential new tethering factors, crucial for endosomal system specificity.

Keywords:
Golgiendocytosisexocytosismembrane contact sitesmembrane fusionrecyclingvesicle trafficking

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Endocytic vesicles fuse with early endosomes, requiring membrane tethering.
  • Specific tethering complexes mediate fusion events within the endosomal system.

Purpose of the Study:

  • To review known tethering complexes involved in endosomal membrane traffic.
  • To discuss the role of tethering factors in ensuring specificity.
  • To highlight the potential existence of novel tethering complexes.

Main Methods:

  • Literature review of endosomal tethering complexes.
  • Analysis of protein delivery pathways within the endosomal system.
  • Identification of potential novel tethering factors.

Main Results:

  • The CORVET complex tethers vesicles to early endosomes.
  • The HOPS complex mediates late endosome-lysosome fusion.
  • GARP and EARP complexes facilitate recycling via TGN and plasma membrane.

Conclusions:

  • Tethering complexes are essential for specific membrane fusion events.
  • Multiple pathways and potential novel factors contribute to endosomal trafficking specificity.