Unraveling How Proteins Are Transported & Sorted in Cells

In summary, the endoplasmic reticulum produces and transports proteins to different parts of the cell. The signal sequence on the growing polypeptide helps the proteins enter the ER. Once the proteins enter the ER, the SRP leaves and translation begins. The growing polypeptide chain is extruded through a pore in the ER membrane and into the lumen of the ER. The signal sequence is usually clipped off the polypeptide, but some proteins, like glycoproteins, are glycosylated and retain the signal sequence. The glycosylation process helps the protein fold into its correct tertiary structure. Sugar residues may also be added to the protein.
  • #1
EIRE2003
108
0
Hi!
If I could get an answer to this question I could understand biology a lot easier. In the cell interior, the endoplasmic Reticulum manufactures proteins and are then transported by a vesicle to the Golgi Apparatus where they are modified or processed and sorted.

My question is, ''how do the molecules know where to go all the time, do they each carry a charge and so are attracted to opposite charges or what?''

And when the proteins are sorted in the Golgi they are tagged, how are they tagged? :confused:
 
Biology news on Phys.org
  • #2
Pathways Through the Endoplasmic Reticulum (ER)
The decision to enter the ER is dictated by the presence of a signal sequence on the growing polypeptide.

The Signal Sequence

The signal sequence consists of the first portion of the elongating polypeptide chain (so the signal sequence occurs at the amino terminal of the polypeptide). Typical signal sequences contain 15 - 30 amino acids. The precise amino acid sequence varies surprisingly from one protein to the next, but all signal sequences include many hydrophobic amino acids.

If a signal sequence is present,

* translation ceases after it has been synthesized
* the signal sequence is recognized by and is bound by a signal recognition particle (SRP)
* the complex of ribosome with its nascent polypeptide and the SRP binds to a receptor on the surface (facing the cytosol) of the ER.
* the SRP leaves and translation recommences
* the growing polypeptide chain is extruded through a pore in the ER membrane and into the lumen of the ER.
* the signal sequence is usually clipped off the polypeptide unless the polypeptide is to be retained as an integral membrane protein.
* other proteins, called molecular chaperones, present in the lumen of the ER, bind the growing polypeptide chain and assist it to fold into its correct tertiary structure.
* sugar residues may be added to the protein. The process is called glycosylation and often is essential for proper folding of the final product, a glycoprotein.

Destinations of proteins synthesized within the ER

The membrane of the transport vesicle fuses with the membrane of the Golgi apparatus, merging their contents. Further steps of glycosylation may occur within the Golgi apparatus. The exact pattern of glycosylation determines the final destination of the proteins. There are two options.

http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/P/ProteinKinesis.html
 
  • #3


Hi there! That's a great question. The process of protein transport and sorting in cells is actually quite complex and involves several different mechanisms. Let's break it down step by step.

Firstly, proteins are synthesized in the endoplasmic reticulum (ER) and then transported to the Golgi apparatus via small membrane-bound structures called vesicles. This process is facilitated by specific signals or "zip codes" located on the proteins themselves, which act as a sort of address to direct them to the correct location. These signals can be recognized by certain proteins or receptors on the vesicle surface, allowing for targeted transport.

Once the proteins reach the Golgi, they are modified and sorted into different vesicles based on their final destination within the cell. This sorting process is also guided by specific signals on the proteins, as well as interactions with other proteins and enzymes within the Golgi.

As for your question about tagging, this refers to the addition of small chemical groups (such as sugars or lipids) onto the proteins. This process, known as post-translational modification, can alter the function or destination of the protein. For example, adding a sugar group can act as a signal for the protein to be transported to a specific organelle or to the cell surface.

Overall, the transport and sorting of proteins in cells is a highly regulated and coordinated process involving a combination of signals, receptors, and modifications. I hope this helps to clarify things for you!
 

1. What is the purpose of protein transportation and sorting in cells?

Protein transportation and sorting is essential for cells to function properly. Proteins are the building blocks of cells and play crucial roles in processes such as metabolism, communication, and defense. Transporting and sorting proteins allows them to reach their specific destinations and carry out their functions.

2. How are proteins transported and sorted in cells?

Proteins are transported and sorted in cells through a complex system involving various organelles, such as the endoplasmic reticulum, Golgi apparatus, and vesicles. Proteins are first synthesized in the endoplasmic reticulum and then transported to the Golgi apparatus, where they are modified and sorted into different vesicles for delivery to their target destinations.

3. What is the role of the endoplasmic reticulum in protein transportation and sorting?

The endoplasmic reticulum is the site of protein synthesis in cells. It also plays a crucial role in protein transportation and sorting by providing a pathway for newly synthesized proteins to reach the Golgi apparatus. The endoplasmic reticulum also helps in folding and modifying proteins before they are transported.

4. How do cells ensure proper protein sorting?

Cells have a specific and highly regulated mechanism for protein sorting. This involves the use of sorting signals, which are specific sequences of amino acids that act as a zip code for proteins, directing them to their correct destination. Additionally, chaperone proteins help in ensuring proper folding and sorting of proteins.

5. What happens if protein transportation and sorting goes wrong?

If protein transportation and sorting go wrong, it can lead to various diseases and disorders. For example, misfolded proteins can accumulate in cells, causing neurodegenerative diseases such as Alzheimer's and Parkinson's. Defects in protein sorting can also lead to conditions such as cystic fibrosis and lysosomal storage disorders.

Similar threads

Replies
4
Views
1K
Replies
4
Views
1K
  • Biology and Medical
Replies
2
Views
3K
  • Biology and Chemistry Homework Help
Replies
4
Views
2K
Replies
8
Views
1K
Replies
13
Views
1K
  • Biology and Chemistry Homework Help
Replies
1
Views
2K
Replies
7
Views
3K
  • Biology and Medical
Replies
7
Views
7K
  • Biology and Chemistry Homework Help
Replies
2
Views
7K
Back
Top