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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.
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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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ER Retrieval Pathway01:45

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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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GPI Anchoring of Proteins in the ER Membrane01:29

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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Post-translational Translocation of Proteins to the RER01:27

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
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The microcephaly-associated protein YIPF5 differentially regulates ER export.

Francesca Bruno1, Mihaela Anitei1, Domenico Di Fraia1

  • 1Leibniz Institute on Aging, Fritz-Lipmann Institute, Beutenbergstr. 11, 07745 Jena, Germany.

Iscience
|February 20, 2026
PubMed
Summary
This summary is machine-generated.

YIPF5 protein regulates ER export, crucial for neuronal development. Its disruption causes microcephaly, epilepsy, and neonatal diabetes syndrome (MEDS2) by affecting protein transport and cell migration.

Keywords:
Cell biologyNeuroscience

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Genetics

Background:

  • YIPF5 is an endoplasmic reticulum (ER) membrane protein involved in ER-Golgi transport.
  • Mutations in YIPF5 lead to MEDS2, a severe early-childhood disorder.
  • YIPF5's precise role in protein export and its link to neurological defects are not fully understood.

Purpose of the Study:

  • To elucidate the function of YIPF5 in ER export and its contribution to neurological development.
  • To investigate the interaction between YIPF5 and the ER export receptor SURF4.
  • To understand the molecular mechanisms underlying YIPF5-associated developmental disorders.

Main Methods:

  • YIPF5 knockout and depletion cell models.
  • Analysis of cell surface protein profiles and secretome.
  • Wound-healing assays to assess cell migration.
  • Immunofluorescence microscopy to study protein localization (ERGIC53, Rab1).
  • Kinetic analysis of ER export.
  • In utero knockdown in mouse embryos.

Main Results:

  • YIPF5 directly interacts with SURF4 and regulates ER export of SURF4 cargoes.
  • YIPF5 deficiency alters cell surface proteins, reducing neuronal adhesion molecules and increasing ER chaperone secretion.
  • YIPF5 depletion enhances cell migration and disrupts SURF4 localization, forming abnormal ER tubules.
  • In utero Yipf5 knockdown causes premature neuronal migration and morphological defects in mouse brains.

Conclusions:

  • YIPF5 and SURF4 collaborate to coordinate the ER export of critical proteins.
  • Disruption of YIPF5 function underlies cortical development defects, potentially causing microcephaly.
  • YIPF5 plays a vital role in regulating neuronal migration and brain development.