Golgi Complex

Discovery

Due to its fairly large size, the golgi apparatus was one of the first organelles to be discovered and observed

in detail. The apparatus was discovered in 1897 by Italian physician Camillo Golgi during an investigation of

the nervous system.

Structure

The Golgi is composed of stacks of membrane-bound structures known as cisternae . An individual stack is

sometimes called a dictyosome. A mammalian cell typically contains 40 to 100 stacks.[6] Between four and

eight cisternae are usually present in a stack; however, in some protists as many as sixty have been

observed.[3] Each cisterna comprises a flattened membrane disk, and carries Golgi enzymes to help or to

modify cargo proteins that travel through them. They are found in both plant and animal cells.

The cisternae stack has four functional regions: the cis-Golgi network, medial-Golgi, endo-Golgi, and trans-
Golgi network. Vesicles from the endoplasmic reticulum (via the vesicular-tubular clusters) fuse with the

network and subsequently progress through the stack to the trans Golgi network, where they are packaged

and sent to the required destination. Each region contains different enzymes which selectively modify the

contents depending on where they reside.[7] The cisternae also carry structural proteins important for their

maintenance as flattened membranes which stack upon each other.

Function

Cells synthesize a large number of different macromolecules. The Golgi apparatus is integral in modifying,
sorting, and packaging these macromolecules for cell secretion (exocytosis) or use within the cell. It
primarily modifies proteins delivered from the rough endoplasmic reticulum but is also involved in the
transport of lipids around the cell, and the creation of lysosomes. In this respect it can be thought of as
similar to a post office; it packages and labels items which it then sends to different parts of the cell.

Enzymes within the cisternae are able to modify substances by the addition of carbohydrates (glycosylation)
and phosphates (phosphorylation). In order to do so, the Golgi imports substances such as nucleotide
sugars from the cytosol. These modifications may also form a signal sequence which determines their final
destination. For example, the Golgi apparatus adds a mannose-6-phosphate label to proteins destined for
lysosomes.

The Golgi plays an important role in the synthesis of proteoglycans, which are molecules present in the
extracellular matrix of animals. It is also a major site of carbohydrate synthesis.[8] This includes the
productions of glycosaminoglycans (GAGs), long unbranched polysaccharides which the Golgi then
attaches to a protein synthesised in the endoplasmic reticulum to form proteoglycans.[9] Enzymes in the
Golgi polymerize several of these GAGs via a xylose link onto the core protein. Another task of the Golgi
involves the sulfation of certain molecules passing through its lumen via sulphotranferases that gain their
sulphur molecule from a donor called PAPs. This process occurs on the GAGs of proteoglycans as well as
on the core protein. The level of sulfation is very important to the proteoglycans' signalling abilities as well as
giving the proteoglycan its overall negative charge.[8]

The phosphorylation of molecules requires that ATP is imported into the lumen of the Golgi[10] and then
utilised by resident kinases such as casein kinase 1 and casein kinase 2. One molecule that is
phosphorylated in the Golgi is Apolipoprotein, which forms a molecule known as VLDL that is a constitute of
blood serum. It is thought that the phosphorylation of these molecules is important to help aid in their sorting
for secretion into the blood serum.[11]
The Golgi has a putative role in apoptosis, with several Bcl-2 family members localised there, as well as to
the mitochondria. A newly characterized protein, GAAP (Golgi anti-apoptotic protein), almost exclusively
resides in the Golgi and protects cells from apoptosis by an as-yet undefined mechanism.[12]