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Related Concept Videos

Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
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Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
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Updated: Jun 2, 2026

Analysis of Tubular Membrane Networks in Cardiac Myocytes from Atria and Ventricles
10:30

Analysis of Tubular Membrane Networks in Cardiac Myocytes from Atria and Ventricles

Published on: October 15, 2014

Fusing a lasting relationship between ER tubules.

Tyler J Moss1, Andrea Daga, James A McNew

  • 1Department of Biochemistry and Cell Biology, Rice University, MS601, Houston, TX 77005, USA.

Trends in Cell Biology
|May 10, 2011
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Atlastin, an endoplasmic reticulum (ER) protein, drives membrane fusion essential for ER structure. Mutations in atlastin-1 cause hereditary spastic paraplegia (HSP), highlighting its role in neuronal health.

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Area of Science:

  • Molecular biology
  • Cell biology
  • Neuroscience

Background:

  • Atlastin is an integral membrane GTPase found in the endoplasmic reticulum (ER).
  • Atlastin functions as a membrane fusogen, crucial for ER structure and maintenance.
  • Mutations in the atlastin-1 gene (SPG3A) are linked to autosomal dominant hereditary spastic paraplegia (HSP).

Purpose of the Study:

  • To review the molecular mechanisms of atlastin function.
  • To explore the role of atlastin in hereditary spastic paraplegia (HSP).
  • To provide insights into ER biogenesis, maintenance, and disease pathology.

Main Methods:

  • In vitro analyses of atlastin function.
  • In vivo studies assessing atlastin's role.
  • Review of existing literature on atlastin and HSP.

Main Results:

  • Atlastin demonstrates membrane fusogenic activity, essential for ER dynamics.
  • Evidence suggests atlastin dysfunction impacts ER structure in motor neurons.
  • Atlastin mutations are implicated in the pathogenesis of hereditary spastic paraplegia.

Conclusions:

  • Understanding atlastin's molecular mechanism is key to deciphering its role in ER maintenance.
  • Atlastin's function is critical for neuronal health, with its dysfunction leading to HSP.
  • Further research into atlastin and related proteins will illuminate ER biogenesis and disease mechanisms.