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Videos de Conceptos Relacionados

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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Vesicular Tubular Clusters01:45

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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.
With the help of motor proteins such...
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ER Retrieval Pathway01:45

ER Retrieval Pathway

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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.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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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
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
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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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Video Experimental Relacionado

Updated: Apr 3, 2026

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
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YIPF5, proteína asociada a la microcefalia, regula diferencialmente la exportación del RE

Francesca Bruno1, Mihaela Anitei1, Domenico Di Fraia1

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

iScience
|February 20, 2026
PubMed
Resumen
Este resumen es generado por máquina.

La proteína YIPF5 regula la exportación del RE, crucial para el desarrollo neuronal. Su alteración causa microcefalia, epilepsia y síndrome de diabetes neonatal (MEDS2) al afectar el transporte de proteínas y la migración celular.

Palabras clave:
Biología celularNeurociencia

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Área de la Ciencia:

  • Biología Celular
  • Neurociencia
  • Genética

Sus antecedentes:

  • YIPF5 es una proteína de la membrana del retículo endoplásmico (RE) involucrada en el transporte RE-Golgi.
  • Las mutaciones en YIPF5 conducen a MEDS2, un trastorno grave de la primera infancia.
  • El papel preciso de YIPF5 en la exportación de proteínas y su vínculo con los defectos neurológicos no se comprenden completamente.

Objetivo del estudio:

  • Elucidar la función de YIPF5 en la exportación del RE y su contribución al desarrollo neurológico.
  • Investigar la interacción entre YIPF5 y el receptor de exportación del RE SURF4.
  • Comprender los mecanismos moleculares subyacentes a los trastornos del desarrollo asociados a YIPF5.

Principales métodos:

  • Modelos celulares de YIPF5 knockout y depleción.
  • Análisis de perfiles de proteínas de superficie celular y secretoma.
  • Ensayos de cicatrización de heridas para evaluar la migración celular.
  • Microscopía de inmunofluorescencia para estudiar la localización de proteínas (ERGIC53, Rab1).
  • Análisis cinético de la exportación del RE.
  • Reducción in utero en embriones de ratón.

Principales resultados:

  • YIPF5 interactúa directamente con SURF4 y regula la exportación del RE de cargas de SURF4.
  • La deficiencia de YIPF5 altera las proteínas de la superficie celular, reduciendo las moléculas de adhesión neuronal y aumentando la secreción de chaperonas del RE.
  • La depleción de YIPF5 mejora la migración celular y altera la localización de SURF4, formando túbulos del RE anormales.
  • La reducción de Yipf5 in utero causa migración neuronal prematura y defectos morfológicos en cerebros de ratón.

Conclusiones:

  • YIPF5 y SURF4 colaboran para coordinar la exportación del RE de proteínas críticas.
  • La alteración de la función de YIPF5 subyace a los defectos del desarrollo cortical, causando potencialmente microcefalia.
  • YIPF5 desempeña un papel vital en la regulación de la migración neuronal y el desarrollo cerebral.