Jove
Visualize
Contáctanos

Videos de Conceptos Relacionados

Golgi Matrix Proteins01:12

Golgi Matrix Proteins

2.5K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.5K
Golgi Apparatus01:49

Golgi Apparatus

105.3K
As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
105.3K
Golgi Apparatus01:09

Golgi Apparatus

22.4K
Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
22.4K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.5K
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...
4.5K
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

5.6K
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,...
5.6K
Transport Across the Golgi01:26

Transport Across the Golgi

6.3K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
6.3K

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

COG Complex in Golgi Trafficking and Glycosylation.

Sub-cellular biochemistry·2026
Same author

Deep proteomic profiling of the intra-Golgi trafficking intermediates.

Molecular biology of the cell·2025
Same author

Acute GARP Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and O-Glycosylation.

Traffic (Copenhagen, Denmark)·2025
Same author

Comprehensive Proteomic Characterization of the Intra-Golgi Trafficking Intermediates.

bioRxiv : the preprint server for biology·2024
Same author

Acute GARP depletion disrupts vesicle transport, leading to severe defects in sorting, secretion, and O-glycosylation.

bioRxiv : the preprint server for biology·2024
Same author

Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>.

mBio·2023
Same journal

Future Directions in Biotechnological and Pharmacological Applications of CAIs.

Sub-cellular biochemistry·2026
Same journal

Industrial and Environmental Applications of Carbonic Anhydrases.

Sub-cellular biochemistry·2026
Same journal

Applications of Carbonic Anhydrase Inhibitors in Arthritis, Neuropathic Pain, Acute Mountain Sickness, and Cerebral Ischemia.

Sub-cellular biochemistry·2026
Same journal

Applications of Carbonic Anhydrase Inhibitors in Neurological Disorders, Mechanisms and Therapeutic Potential.

Sub-cellular biochemistry·2026
Same journal

Carbonic Anhydrase Inhibitors in Oncology.

Sub-cellular biochemistry·2026
Same journal

Therapeutic Applications of Carbonic Anhydrase Inhibitors in Ophthalmology.

Sub-cellular biochemistry·2026
Ver todos los artículos relacionados
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Video Experimental Relacionado

Updated: Feb 22, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

11.4K

Complejo GARP en la fisiología de Golgi

Amrita Khakurel1, Walter S Aragon-Ramirez1, Vladimir V Lupashin2

  • 1Department of Physiology and Cell Biology, University of Arkansas for Medical Sciences, Little Rock, AR, USA.

Sub-cellular biochemistry
|February 20, 2026
PubMed
Resumen
Este resumen es generado por máquina.

El complejo de la proteína retrógrada asociada a Golgi (GARP) es crucial para el transporte de las vesículas desde los endosomas hasta el Golgi. Cómo entender el GARP

Palabras clave:
El tráfico retrógrado del endosoma-TGN.GARP es el nombre que se le da a la garpa.La glucosilación por glicosilaciónMaquinaria para el tráfico de personas.La conexión de las vesículas.

Más Videos Relacionados

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
11:05

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Published on: February 21, 2019

9.7K
Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
10:12

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells

Published on: May 21, 2014

18.8K

Videos de Experimentos Relacionados

Last Updated: Feb 22, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

11.4K
Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
11:05

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Published on: February 21, 2019

9.7K
Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
10:12

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells

Published on: May 21, 2014

18.8K

Área de la Ciencia:

  • Biología celular Biología celular.
  • Biología Molecular Biología Molecular
  • Genética La genética.

Sus antecedentes:

  • El complejo de proteína retrógrada asociada a Golgi (GARP), parte de la familia CATCHR, media el enlace de las vesículas de los endosomas a la red trans-Golgi (TGN).
  • GARP es vital para la clasificación de hidrolasas y el reciclaje de proteínas de membrana, pero sus mecanismos precisos, socios y intermediarios de tráfico son poco estudiados.
  • Las vías dependientes de GARP se utilizan para reciclar proteínas, receptores de hidrolasa y patógenos, con mutaciones vinculadas a trastornos neurológicos.

Objetivo del estudio:

  • Revisar los conocimientos actuales sobre la estructura, función e interacciones del complejo GARP.
  • Resumir el impacto de las mutaciones de GARP y su asociación con patologías humanas.
  • Para resaltar los aspectos poco estudiados del tráfico dependiente de GARP.

Principales métodos:

  • Revisión de la literatura de los estudios existentes sobre el complejo GARP.
  • Análisis de la investigación sobre el papel de GARP en la clasificación de proteínas y el reciclaje de membranas.
  • Compilación de datos sobre mutaciones de GARP y trastornos neurológicos asociados en humanos y organismos modelo.

Principales resultados:

  • Las funciones del complejo GARP en el tráfico retrógrado de endosoma a TGN.
  • El transporte dependiente de GARP es esencial para varios procesos celulares y explotado por los patógenos.
  • Las mutaciones en las subunidades de GARP están implicadas en enfermedades neurológicas, aunque los mecanismos no están claros.

Conclusiones:

  • El complejo GARP juega un papel crítico en las vías de tráfico celular.
  • Se necesita más investigación para dilucidar los mecanismos moleculares exactos de GARP y las asociaciones de enfermedades.
  • La comprensión de GARP es vital para la comprensión de la función celular normal y la patogénesis de los trastornos neurológicos.