Exact(4)
A protein generally undergoes the following process to be ready to move out of a cell: protein biosynthesis, translocation to endoplasmic reticulum, attachment of N-glycan, glycoprotein folding, N- and O-glycosylation, transportation to Golgi apparatus, protein sorting and formation of secretory vesicles, vesicle budding, transport, and vesicle fusion with the plasma membrane [ 13, 14].
Dynamin is a large GTPase protein involved in cell and organellar membrane budding, transport and fission [38].
So far, in humans, the Rab family has been shown to have more than 60 proteins scattered around distinct intracellular compartments, where they regulate vesicle budding, transport and fusion [9], [10].
Vesicles enclose these molecules; undergo budding, transport and tethering; and finally fuse with the plasma membrane to release their contents.
Similar(56)
Membrane trafficking is an intracellular system that can be used to transport proteins; this process includes steps such as budding of transport vesicles in organelles and vesicular fusion to target membrane.
Rab7 regulates transport of growth factors and other cargo from early to late endosomes and on to lysosomes by controlling membrane budding, cytoskeletal transport and fusion between endocytic compartments.
The budding of transport vesicles from the Golgi complex is initiated by activation of the small GTPase ARF; the discovery of enzymes that can convert soluble ARF-GDP to the active, membrane-associated form ARF-GTP will shed light on the mechanism and regulation of the formation of transport vesicles.
In S. cerevisiae, Sfb3 is involved in vesicle budding and transport of cargo from the ER but not vesicle fusion with the Golgi body.
These findings are in line with the postulated role of CK1 family members in regulating vesicle budding and transport processes [1], [2], [19], [56], [57].
The COPI coat is localized to Golgi membranes, where it drives the budding of transport vesicles that mediate Golgi-to-ER retrieval and intra-Golgi traffic.
In the same line, G1 cells could be depleted of GM130 or GRASP proteins and examined to determine whether the budding of transport vesicles or trafficking of specific cargoes from the fragmented Golgi is affected by Golgi structure.
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