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Related Concept Videos

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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SNAREs and Membrane Fusion01:43

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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.
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Overview of Secretory Vesicles01:33

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Intralumenal Vesicles and Multivesicular Bodies01:38

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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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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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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Related Experiment Video

Updated: Jun 17, 2025

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
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The Ribosome Assembly Factor LSG1 Interacts with Vesicle-Associated Membrane Protein-Associated Proteins (VAPs).

Putri Sutjita1, Sharmishtha Musalgaonkar2, Jeffrey Recchia-Rife2

  • 1Interdisciplinary Life Sciences Graduate Program, The University of Texas at Austin, Austin, Texas, USA.

Molecular and Cellular Biology
|August 12, 2024
PubMed
Summary

Human LSG1 protein binds to VAPs at the endoplasmic reticulum via a novel motif. This interaction is crucial for LSG1

Keywords:
LSG1Ribosome biogenesisVAPvesicle-associated membrane protein-associated protein

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • LSG1 is a GTPase essential for ribosome biogenesis, specifically the removal of the NMD3 adapter from pre-60S ribosomal subunits.
  • LSG1 interacts with vesicle-associated membrane protein-associated proteins (VAPs) located on the endoplasmic reticulum (ER).
  • VAPs bind proteins with FFAT motifs, mediating functions in membrane traffic and lipid transport.

Purpose of the Study:

  • To investigate the mechanism by which human LSG1 localizes to the ER.
  • To determine if LSG1 utilizes an FFAT motif to interact with VAPs.
  • To assess the functional consequences of disrupting the LSG1-VAP interaction.

Main Methods:

  • Analysis of human LSG1 protein interactions with VAPs.
  • Identification and deletion of a noncanonical FFAT-like motif in LSG1.
  • Cellular localization studies of wild-type and mutant LSG1.
  • Assays for NMD3 recycling and LSG1 GTPase activity.

Main Results:

  • Human LSG1 binds to VAPs through a noncanonical FFAT-like motif.
  • Deletion of this motif abolishes LSG1 localization to the ER.
  • Disruption of the motif does not affect NMD3 recycling or LSG1 GTPase activity.

Conclusions:

  • LSG1 utilizes a unique FFAT-like motif for ER targeting via VAP interaction.
  • ER localization of LSG1 is separable from its role in NMD3 recycling and GTPase function.
  • This finding reveals a specific mechanism for regulating LSG1 localization independent of its core ribosome assembly function.