multivesicular body

These multivesicular bodies eventually fuse with the lysosome causing degradation of the cargo.

It is because of these vesicles that the endosome is sometimes known as a multivesicular body.

Multivesicular bodies play a large role in the transport of ubiquitinated proteins and receptors to a lysosome.

First of these mechanisms is exocytosis from multivesicular bodies and the formation of exosomes.

There is also growing evidence of a large number of multivesicular bodies and other lysosomal components seen in these cells, indicating a high endocytic activity.

Once formed, the endosome combines with a structure known as a multivesicular body (MVB).

Multivesicular bodies are endosomal compartments that sort ubiquitinated membrane proteins by incorporating them into vesicles.

Vesicular mechanism can use lysosome-dependent pathway, microvesicle shedding or biogenesis of multivesicular bodies.

Multivesicular body, or MVB, is a membrane-bound vesicle containing a number of smaller vesicles.

Charged multivesicular body protein 3 is a protein that in humans is encoded by the VPS24 gene.

Back-fusion is the fusion of internal (intraluminal) vesicles within multivesicular bodies or late endosomes with the endosome's limiting membrane.

Such endosomes are called multivesicular bodies because of their appearance, with many small vesicles, or "intralumenal endosomal vesicles," inside the larger body.

This results in the removal of ubiquitin tags from proteins targeted for degradation in the lysosome just prior to the generation of multivesicular bodies.

CHMP5 belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family.

The intralumenal endosomal vesicles become exosomes if the multivesicular body merges with the cell membrane, releasing the internal vesicles into the extracellular space.

Exosomes are either released from the cell when multivesicular bodies fuse with the plasma membrane or they are released directly from the plasma membrane.

Multivesicular body (MVB) biogenesis is a process in which ubiquitin tagged proteins enter organelles called endosomes via the formation of vesicles.

Once properly localized, these proteins are then taken into the endosome via vesicles, forming multivesicular bodies, and are eventually delivered to the lysosome where they are degraded.

ESCRT complexes transport ubiquitinated cargo to cellular vesicles that bud directly into the cell's endosomal compartment, forming multivesicular bodies.

Mitochondria, endoplasmic reticulum, Golgi apparatus and multivesicular bodies all appear to swell, though this can be best seen in the mitochondria which appear to swell first.

This Vps4-Vta1 complex triggers the disassembly of ESCRT-III and marks the end of multivesicular body formation.

The ESCRT-II complex functions primarily during the biogenesis of multivesicular bodies and delivery of ubiquitin tagged proteins to the endosome.

ESCRT machinery plays a vital role in a number of cellular processes including multivesicular body (MVB) biogenesis, cellular abscission, and viral budding.

The ESCRT-0 complex plays a vital role in the generation of multivesicular bodies by binding and clustering ubiquitinated proteins and/or receptors on the surface of a cell.

These filamentous structures are also present during multivesicular body formation and function as a ring-like fence that plugs the budding vesicle to prevent cargo proteins from escaping into the cell's cytosol.