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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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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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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.
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TECPR2 Cooperates with LC3C to Regulate COPII-Dependent ER Export.

Daniela Stadel1, Valentina Millarte2, Kerstin D Tillmann2

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Tectonin β-propeller containing protein 2 (TECPR2) links cellular secretion and autophagy pathways. This discovery clarifies TECPR2

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Area of Science:

  • Molecular Biology
  • Neurodegenerative Diseases
  • Cellular Trafficking

Background:

  • Hereditary spastic paraplegias (HSPs) are neurodegenerative disorders affecting corticospinal motor neurons.
  • Mutations in TECPR2 cause HSP with neurological complications.
  • TECPR2's precise function, despite being an autophagy regulator, remains unclear.

Purpose of the Study:

  • To elucidate the molecular function of TECPR2 in cellular pathways.
  • To investigate TECPR2's role in the early secretion pathway and autophagy.
  • To understand the mechanism by which TECPR2 mutations lead to HSP.

Main Methods:

  • Investigated TECPR2 interactions with trafficking components, including SEC24D.
  • Assessed TECPR2's requirement for SEC24D stabilization, ER exit sites (ERES) maintenance, and ER export.
  • Analyzed TECPR2 and LC3C involvement in autophagosome formation using TECPR2-deficient cells.

Main Results:

  • TECPR2 associates with SEC24D and is crucial for its protein levels and functional ERES.
  • TECPR2 facilitates efficient ER export, dependent on its binding to lipidated LC3C.
  • TECPR2-deficient cells show altered SEC24D levels, impaired ER export, and defective autophagosome formation.

Conclusions:

  • TECPR2 acts as a molecular scaffold connecting the early secretion pathway and autophagy.
  • TECPR2's function is vital for maintaining cellular homeostasis and preventing neurodegeneration in HSP.
  • Dysregulation of TECPR2 impacts both ER export and autophagosome formation, contributing to HSP pathogenesis.