Which of the following most accurately explains why the golgi complex is often near the rough er?

61 With the SER, RER, lysosomes, other intermediate organelle compartments, and even the nuclear and mitochondrial envelope membranes, the Golgi is an integral part of the complex intracellular organelle network involving vesicular trafficking that enables uptake, sorting, degradation, biosynthesis, trafficking, and/or secretion of cellular proteins and lipids.

From: Zakim and Boyer's Hepatology (Seventh Edition), 2018

Which of the following most accurately explains why the golgi complex is often near the rough er?

The Golgi body (or Golgi complex, apparatus), and Endoplasmic reticulum (ER) are both organelles found in the majority of eukaryotic cells.  They are very closely associated and show both similarities and differences in structure and function. Some of these are as follows:

Structure

The Golgi body consists of stacks of flattened membrane-enclosed and fluid-filled saccules (cisternae). It is also associated with tubules continuous with the edges of the saccules and vesicles. Unlike the ER, the Golgi shows both structural and functional polarization.

Which of the following most accurately explains why the golgi complex is often near the rough er?

Golgi apparatus. Golgi Complex plays an important role in the modification and transport of proteins within the cell. Image Copyright: Designua / Shutterstock

It is not entirely understood how this is maintained however it seems to underlie the directional flow of materials from the cis (input) to the trans (output) cisternae amongst other forms of transport. It might also explain how the secretory vesicles form on the cis face of the Golgi and mature and dissociate from the trans face on the opposite side of the stack.

Which of the following most accurately explains why the golgi complex is often near the rough er?

Endoplasmic reticulum is a continuous membrane, which is present in both plant cells, animal cells and absent in prokaryotic. Image Copyright: Designua / Shutterstock

Similarly, the ER comprises an extensive network of  membrane-enclosed sacs and tubules. It has such a physically wide reach that in most eukaryotic cells, it is the largest organelle.  It also has a much larger internal structure than the Golgi body to carry out its activities.

There are two distinct sub-compartments of the ER – the rough and the smooth ER.

The rough ER is characterized by fairly flat, sealed sacs which are studded with membrane-bound ribosomes on the outer surface (which is exposed to the cytosol).

In contrast, the smooth ER has a more tubular structure and does not have ribosomes on its surface hence its smooth appearance.

As the ER is composed of the distinct rough and smooth surfaces, the organelle has numerous diverse functions.

The rough ER is required for the folding and processing of membrane, transmembrane and secreted proteins. More specifically, chaperone proteins within the ER assist in folding polypeptide chains into their three-dimensional structures. Further modifications such as disulfide bridge formation or glycosylation may follow before the proteins undergo quality control then export to other sites such as the Golgi.

In contrast to the function of the rough ER, the smooth ER is important in the synthesis of membrane lipids or their precursors i.e. for glycerol phospholipids, ceramide and cholesterol.

Additionally, the smooth ER is involved in the metabolism of lipids via the production of steroid hormones (from cholesterol) and lipid-soluble compounds through its resident enzymes.

Some of these structurally appropriate lipids and glycoproteins are exported into the Golgi.

The Golgi has a similar but perhaps more extensive role than the ER – it is required for glycoprotein processing through the synthesis and subsequent addition of carbohydrate residues i.e. glycosylation. Glycoproteins which have been processed and imported from the ER may be subject to even further alteration in the Golgi.

Lipid metabolism also occurs in the Golgi. This involves using ceramide synthesized and imported from the ER to synthesize sphingomyelin and glycolipids.

Following the synthesis of these modified compounds, the Golgi sorts them into different kinds of transport vesicles to deliver their contents to their cellular destinations — either lysosomes, or the plasma membrane or are retained within the Golgi.

Relationship with Lysosomes

Lysosomes are membrane-bound organelles containing a repertoire of hydrolytic enzymes called acid hydrolases. These have the ability to digest intracellular macromolecules such as proteins, lipids and sugars.

The functioning of the Golgi apparatus and ER are both so closely linked to the lysosomes that together, these entities compose the endomembrane system. Interestingly, lysosomal formation relies on the joint contribution of the ER and Golgi.

The Golgi is responsible for the formation of lysosomes. When vesicles bud off from the trans-Golgi and fuse with endosomes, lysosomes are formed.

In contrast, the ER is where the lysosomal hydrolases are synthesized. Then they are transported to the Golgi, and are tagged for the lysosomes by the addition of mannose-6-phosphate label.

Intracellular Location

Part of the ER is continuous with the nuclear envelope of the cell. More specifically, the density of rough ER is higher near the nucleus and Golgi apparatus whilst the smooth ER seems to be located evenly throughout the cell.

On the other hand, the Golgi is not directly associated with the nucleus – instead, it is located in the cytosol of the cell in close proximity to the rough ER (therefore, also near the nucleus of the cell).

References

Further Reading

Last updated Jul 19, 2019

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Home Science Biology Cells, Organs & Tissues

The Golgi apparatus, also called Golgi complex or Golgi body, is a membrane-bound organelle found in eukaryotic cells (cells with clearly defined nuclei) that is made up of a series of flattened stacked pouches called cisternae. It is located in the cytoplasm next to the endoplasmic reticulum and near the cell nucleus. While many types of cells contain only one or several Golgi apparatus, plant cells can contain hundreds.

The Golgi apparatus is responsible for transporting, modifying, and packaging proteins and lipids into vesicles for delivery to targeted destinations. As the secretory proteins move through the Golgi apparatus, a number of chemical modifications may transpire. Important among these is the modification of carbohydrate groups. Also within the Golgi or secretory vesicles are proteases that cut many secretory proteins at specific amino acid positions.

Learn more about cell organelles.

The Golgi apparatus was observed in 1897 by Italian cytologist Camillo Golgi. In Golgi’s early studies of nervous tissue, he established a staining technique that he referred to as reazione nera, meaning “black reaction”; today it is known as the Golgi stain. In this technique, nervous tissue is fixed with potassium dichromate and then suffused with silver nitrate. While examining neurons that he stained by using his black reaction, Golgi identified an “internal reticular apparatus.” This structure became known as the Golgi apparatus, though some scientists questioned whether the structure was real and attributed the find to free-floating particles of Golgi’s metal stain. In the 1950s, however, when the electron microscope came into use, the existence of the Golgi apparatus was confirmed.

In general, the Golgi apparatus is made up of approximately four to eight cisternae, although in some single-celled organisms it may consist of as many as 60 cisternae. The cisternae are held together by matrix proteins, and the whole of the Golgi apparatus is supported by cytoplasmic microtubules. The apparatus has three primary compartments, known generally as “cis,” “medial,” and “trans.” The cis Golgi network and the trans Golgi network, which are made up of the outermost cisternae at the cis and trans faces, are structurally polarized. The cis face lies near the transitional region of the rough endoplasmic reticulum, while the trans face lies near the cell membrane. These two networks are responsible for the essential task of sorting proteins and lipids that are received (at the cis face) or released (at the trans face) by the organelle. The cis face membranes are generally thinner than the others.

Golgi apparatus, also called Golgi complex or Golgi body, membrane-bound organelle of eukaryotic cells (cells with clearly defined nuclei) that is made up of a series of flattened, stacked pouches called cisternae. The Golgi apparatus is responsible for transporting, modifying, and packaging proteins and lipids into vesicles for delivery to targeted destinations. It is located in the cytoplasm next to the endoplasmic reticulum and near the cell nucleus. While many types of cells contain only one or several Golgi apparatus, plant cells can contain hundreds.

Secretory proteins and glycoproteins, cell membrane proteins, lysosomal proteins, and some glycolipids all pass through the Golgi apparatus at some point in their maturation. In plant cells, much of the cell wall material passes through the Golgi as well.

The Golgi apparatus itself is structurally polarized, with three primary compartments lying between the “cis” face and the “trans” face. These faces are biochemically distinct, and the enzymatic content of each segment is markedly different. The cis face membranes are generally thinner than the others.

In general, the Golgi apparatus is made up of approximately four to eight cisternae, although in some single-celled organisms it may consist of as many as 60 cisternae. The cisternae are held together by matrix proteins, and the whole of the Golgi apparatus is supported by cytoplasmic microtubules. The three primary compartments of the apparatus are known generally as “cis” (cisternae nearest the endoplasmic reticulum), “medial” (central layers of cisternae), and “trans” (cisternae farthest from the endoplasmic reticulum). Two networks, the cis Golgi network and the trans Golgi network, which are made up of the outermost cisternae at the cis and trans faces, are responsible for the essential task of sorting proteins and lipids that are received (at the cis face) or released (at the trans face) by the organelle.

Which of the following most accurately explains why the golgi complex is often near the rough er?

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Golgi apparatus: exocytosis

The proteins and lipids received at the cis face arrive in clusters of fused vesicles. These fused vesicles migrate along microtubules through a special trafficking compartment, called the vesicular-tubular cluster, that lies between the endoplasmic reticulum and the Golgi apparatus. When a vesicle cluster fuses with the cis membrane, the contents are delivered into the lumen of the cis face cisterna. As proteins and lipids progress from the cis face to the trans face, they are modified into functional molecules and are marked for delivery to specific intracellular or extracellular locations. Some modifications involve cleavage of oligosaccharide side chains followed by attachment of different sugar moieties in place of the side chain. Other modifications may involve the addition of fatty acids or phosphate groups (phosphorylation) or the removal of monosaccharides.

The different enzyme-driven modification reactions are specific to the compartments of the Golgi apparatus. For example, the removal of mannose moieties occurs primarily in the cis and medial cisternae, whereas the addition of galactose or sulfate occurs primarily in the trans cisternae. In the final stage of transport through the Golgi apparatus, modified proteins and lipids are sorted in the trans Golgi network and are packaged into vesicles at the trans face. These vesicles then deliver the molecules to their target destinations, such as lysosomes or the cell membrane.

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Some molecules, including certain soluble proteins and secretory proteins, are carried in vesicles to the cell membrane for exocytosis (release into the extracellular environment). The exocytosis of secretory proteins may be regulated, whereby a ligand must bind to a receptor to trigger vesicle fusion and protein secretion. In addition, within the vesicles are proteases that cut many secretory proteins at specific amino acid positions. This often results in activation of the secretory protein, an example being the conversion of inactive proinsulin to active insulin by removing a series of amino acids.

Some secretory proteins will cease to be transported if their carbohydrate groups are modified incorrectly or are not permitted to form. In some cases the carbohydrate groups are necessary for the stability or activity of the protein or for targeting the molecule for a specific destination.