thumb|300px|Diagram of a single "stack" of Golgi
The Golgi apparatus (), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. Part of the endomembrane system in the cytoplasm, it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus.
The Golgi apparatus was identified in 1898 by the Italian biologist and pathologist Camillo Golgi. The organelle was later named after him in the 1910s. After first observing it under his microscope, he termed the structure as apparato reticolare interno ("internal reticular apparatus"). Some doubted the discovery at first, arguing that the appearance of the structure was merely an optical illusion created by Golgi's observation technique. With the development of modern microscopes in the twentieth century, the discovery was confirmed. Early references to the Golgi apparatus referred to it by various names, including the Golgi–Holmgren apparatus, Golgi–Holmgren ducts, and Golgi–Kopsch apparatus. In yeast, multiple Golgi apparatuses are scattered throughout the cytoplasm (as observed in Saccharomyces cerevisiae). In plants, Golgi stacks are not concentrated at the centrosomal region and do not form Golgi ribbons. Organization of the plant Golgi depends on actin cables and not microtubules.
Structure
thumb|left|3D rendering of Golgi apparatus
In most eukaryotes, the Golgi apparatus is made up of a series of compartments and is a collection of fused, flattened membrane-enclosed disks known as cisternae (singular: cisterna, also called "dictyosomes"), originating from vesicular clusters that bud off the endoplasmic reticulum (ER). A mammalian cell typically contains 40 to 100 stacks of cisternae. Between four and eight cisternae are usually present in a stack; however, in some protists, as many as sixty cisternae have been observed.
There are structural and organizational differences in the Golgi apparatus among eukaryotes. In some yeasts, Golgi stacking is not observed. Pichia pastoris does have stacked Golgi, while Saccharomyces cerevisiae does not.
In all eukaryotes, each cisternal stack has a cis entry face and a trans exit face. These faces are characterized by unique morphology and biochemistry. Within individual stacks are assortments of enzymes responsible for selectively modifying protein cargo. These modifications influence the fate of the protein. The compartmentalization of the Golgi apparatus is advantageous for separating enzymes, thereby maintaining consecutive and selective processing steps: enzymes catalyzing early modifications are gathered in the cis face cisternae, and enzymes catalyzing later modifications are found in trans face cisternae of the Golgi stacks.
The structure and function of the Golgi apparatus are intimately linked. Individual stacks have different assortments of enzymes, allowing for progressive processing of cargo proteins as they travel from the cisternae to the trans Golgi face. and phosphates (phosphorylation). Protein modifications may form a signal sequence that determines the final destination of the protein. For example, the Golgi apparatus adds a mannose-6-phosphate label to proteins destined for lysosomes. Another important function of the Golgi apparatus is in the formation of proteoglycans. Enzymes in the Golgi append proteins to glycosaminoglycans, thus creating proteoglycans. Glycosaminoglycans are long unbranched polysaccharide molecules present in the extracellular matrix of animals.
Vesicular transport
thumb|315px|Diagram of secretory process from endoplasmic reticulum (orange) to Golgi apparatus (magenta). 1. [[Nuclear membrane; 2. Nuclear pore; 3. Rough endoplasmic reticulum (RER); 4. Smooth endoplasmic reticulum (SER); 5. Ribosome attached to RER; 6. Macromolecules; 7. Transport vesicles; 8. Golgi apparatus; 9. Cis face of Golgi apparatus; 10. Trans face of Golgi apparatus; 11. Cisternae of the Golgi apparatus.]]
The vesicles that leave the rough endoplasmic reticulum are transported to the cis face of the Golgi apparatus, where they fuse with the Golgi membrane and empty their contents into the lumen. Once inside the lumen, the molecules are modified, then sorted for transport to their next destinations.
Those proteins destined for areas of the cell other than either the endoplasmic reticulum or the Golgi apparatus are moved through the Golgi cisternae towards the trans face, to a complex network of membranes and associated vesicles known as the trans-Golgi network (TGN). This area of the Golgi is the point at which proteins are sorted and shipped to their intended destinations by their placement into one of at least three different types of vesicles, depending upon the signal sequence they carry.
{| class="wikitable"
! Types
! Description
! Example
|-
! Exocytotic vesicles (constitutive)
| Vesicle contains proteins destined for extracellular release. After packaging, the vesicles bud off and immediately move towards the plasma membrane, where they fuse and release the contents into the extracellular space in a process known as constitutive secretion.
| Antibody release by activated plasma B cells
|-
! Secretory vesicles (regulated)
| Vesicles contain proteins destined for extracellular release. After packaging, the vesicles bud off and are stored in the cell until a signal is given for their release. When the appropriate signal is received they move toward the membrane and fuse to release their contents. This process is known as regulated secretion.
| Neurotransmitter release from neurons
|-
! Lysosomal vesicles
| Vesicles contain proteins and ribosomes destined for the lysosome, a degradative organelle containing many acid hydrolases, or to lysosome-like storage organelles. These proteins include both digestive enzymes and membrane proteins. The vesicle first fuses with the late endosome, and the contents are then transferred to the lysosome via unknown mechanisms.
| Digestive proteases destined for the lysosome
|}
Current models of vesicular transport and trafficking
Model 1: Anterograde vesicular transport between stable compartments
- In this model, the Golgi is viewed as a set of stable compartments that work together. Each compartment has a unique collection of enzymes that work to modify protein cargo. Proteins are delivered from the ER to the cis face using COPII-coated vesicles. Cargo then progress toward the trans face in COPI-coated vesicles. This model proposes that COPI vesicles move in two directions: anterograde vesicles carry secretory proteins, while retrograde vesicles recycle Golgi-specific trafficking proteins.
- Strengths: The model explains observations of compartments, polarized distribution of enzymes, and waves of moving vesicles. It also attempts to explain how Golgi-specific enzymes are recycled.
- Strengths: This model encompasses the strengths of the cisternal progression/maturation model that also explains rapid trafficking of cargo, and how native Golgi proteins can recycle independently of COPI vesicles. BFA blocks the activation of some ADP-ribosylation factors (ARFs). ARFs are small GTPases which regulate vesicular trafficking through the binding of COPs to endosomes and the Golgi.
File:GolgiRibbonc.jpg|Two Golgi stacks connected as a ribbon in a mouse cell. Taken from the movie.
File:GolgiScyl1c.jpg|Three-dimensional projection of a mammalian Golgi stack imaged by confocal microscopy and volume surface rendered using Imaris software. Taken from the movie.
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