Membrane vesicle trafficking

Résumé

Membrane vesicle trafficking in eukaryotic animal cells involves movement of biochemical signal molecules from synthesis-and-packaging locations in the Golgi body to specific release locations on the inside of the plasma membrane of the secretory cell. It takes place in the form of Golgi membrane-bound micro-sized vesicles, termed membrane vesicles (MVs). In this process, the packed cellular products are released or secreted outside the cell, across its plasma membrane. On the other hand, the vesicular membrane is retained and recycled by the secretory cells. This phenomenon has a major role in synaptic neurotransmission, endocrine secretion, mucous secretion, granular-product secretion by neutrophils, and other phenomena. The scientists behind this discovery were awarded Nobel prize for the year 2013. In prokaryotic, gram-negative bacterial cells, membrane vesicle trafficking is mediated through bacterial outer membrane bounded nano-sized vesicles, called bacterial outer membrane vesicles (OMVs). In this case, however, the OMV membrane is secreted as well, along with OMV-contents to outside the secretion-active bacterium. This different phenomenon has a major role in host-pathogen interactions, endotoxic shock in patients, invasion and infection of animals or plants, inter-species bacterial competition, quorum sensing, exocytosis, and other areas. Once vesicles are produced in the endoplasmic reticulum and modified in the golgi body they make their way to a variety of destinations within the cell. Vesicles first leave the golgi body and are released into the cytoplasm in a process called budding. Vesicles are then moved towards their destination by motor proteins. Once the vesicle arrives at its destination it joins with the bi-lipid layer in a process called fusion, and then releases its contents. Receptors embedded in the membrane of the golgi body bind specific cargo (such as dopamine) on the lumenal side of the vesicle. These cargo receptors then recruit a variety of proteins including other cargo receptors and coat proteins such as clathrin, COPI and COPII.

Source officielle

https://en.wikipedia.org/wiki/Membrane_vesicle_trafficking

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Publications associées (4)

Personnes associées (2)

Giovanni D'Angelo, Françoise Gisou van der Goot Grunberg

Unités associées (1)

Concepts associés (21)

Outer membrane vesicles

Outer membrane vesicles (OMVs) are vesicles released from the outer membranes of Gram-negative bacteria. While Gram-positive bacteria release vesicles as well those vesicles fall under the broader category of bacterial membrane vesicles (MVs). OMVs were the first MVs to be discovered, and are distinguished from outer inner membrane vesicles (OIMVS), which are gram-negitive baterial vesicles containing portions of both the outer and inner bacterial membrane.

Membrane vesicle trafficking

Sécrétion

La sécrétion est une action conduisant une cellule à envoyer dans le milieu extracellulaire une substance (hormone, neurotransmetteur, glycoprotéines). Le processus de sécrétion implique la fusion de vésicules (contenant la substance à sécréter) avec la membrane cytoplasmique (ou membrane plasmique) de la cellule, libérant ainsi le contenu de la vésicule à l'extérieur de la cellule. Par extension, la sécrétion désigne aussi le produit sécrété.

Cours associés (17)

Séances de cours associées (83)

Connecting vesicular transport with lipid synthesis: FAPP2

Giovanni D'Angelo

Next to the protein-based machineries composed of small G-proteins, coat complexes, SNAREs and tethering factors, the lipid-based machineries are emerging as important players in membrane trafficking. As a component of these machineries, lipid transfer proteins have recently attracted the attention of cell biologists for their involvement in trafficking along different segments of the secretory pathway. Among these, the four-phosphate adaptor protein 2 (FAPP2) was discovered as a protein that localizes dynamically with the trans-Golgi network and regulates the transport of proteins from the Golgi complex to the cell surface. Later studies have highlighted a role for FAPP2 as lipid transfer protein involved in glycosphingolipid metabolism at the Golgi complex. Here we discuss the available evidence on the function of FAPP2 in both membrane trafficking and lipid metabolism and propose a mechanism of action of FAPP2 that integrates its activities in membrane trafficking and in lipid transfer. This article is part of a Special Issue entitled Lipids and Vesicular Transport.

2012

GRASP65 and GRASP55 Sequentially Promote the Transport of C-terminal Valine-bearing Cargos to and through the Golgi Complex

Giovanni D'Angelo

The Golgi matrix proteins GRASP65 and GRASP55 have recognized roles in maintaining the architecture of the Golgi complex, in mitotic progression and in unconventional protein secretion whereas, surprisingly, they have been shown to be dispensable for the transport of commonly used reporter cargo proteins along the secretory pathway. However, it is becoming increasingly clear that many trafficking machineries operate in a cargo-specific manner, thus we have investigated whether GRASPs may control the trafficking of selected classes of cargo. We have taken into consideration the C-terminal valine-bearing receptors CD8alpha and Frizzled4 that we show bind directly to the PSD95-DlgA-zo-1 (PDZ) domains of GRASP65 and GRASP55. We demonstrate that both GRASPs are needed sequentially for the efficient transport to and through the Golgi complex of these receptors, thus highlighting a novel role for the GRASPs in membrane trafficking. Our results open new perspectives for our understanding of the regulation of surface expression of a class of membrane proteins, and suggests the causal mechanisms of a dominant form of autosomal human familial exudative vitreoretinopathy that arises from the Frizzled4 mutation involving its C-terminal valine.

2009

Function and dysfunction of the PI system in membrane trafficking

Giovanni D'Angelo

2008