What are phosphorylation sites?

Phosphorylation sites are specific areas of molecules that are subject to the addition or removal of the phosphate group known as PO4. They are particularly important for the control of protein in the cell. Phosphorylation may activate or deactivate protein and is an important way to regulate paths in the cell. One protein can have many phosphorylation sites and each individual cell can have thousands. Some phosphorylation results that have disappeared may include cancer and diabetes. Protein phosphorylation may change its function or location in the cell. Individual enzymes differ in whether their active form has phosphorylation site phosphorylated or empty.

receptors are also important places in phosphorylation. These transmission signals and transduction paths of the signal are often regulated by phosphorylation sites. One of the factors that are beneficial to regulate that the timing of signaling reactions may vary from less than a second. Paths of phosphorylation can be very complex with a series of proteins of sequential phosphorylaCE of another. This leads to the amplification of the track.

Protein that adds phosphate is called kinase . These regulate a large number of reactions in the cell. Proteins that remove the group of phosphoryl are called phosphatases .

kinases obtain a phosphate group from adenosine triposphate (ATP). They add a group of phosphate to one of the three amino acids - serine, threonin or tyrosine. Others can act on all three or even other amino acids such as histidine. Some kinases have more specifics and can affect more than one goal. Such a wide target specificity allows coordinated regulation more paths.

One of the very important subgroups of kinase is serine/threonine protein kinase . Their phosphorylation site is an OH group of serine or threonin. Phosphorylation by these kinases can be regulated by chemical signals and also by events suchDNA. Map kinases are a well -studied group of this type and map kinase subgroup is called kinases regulated by extracellular signal (ERK).

Phosphorylation

Erk is widely expressed as an intracellular signaling mechanism. What is important in these ERK kinases is that they transmit extracellular signals and intensify them inside the cell. The road is activated by many different extracellular factors, including growth factors, hormones and carcinogens. The ERK path is disturbed in many cancer.

It is a highly active study of study. Up to half of the proteins in the cell can be phosphorylated. Different compania specializes in predicting which protein areas can be phosphorylated.

The protein phosphorylation test generally uses antibodies. These are proteins produced by the immune system of the animal that are specific to foreign attackers. There are hundreds of antibodies that are specific to structural ZMmade by phosphorylation. The proteins are operated on a gel that is separated by size and charge and is known as two -dimensional electrophoresis. It is then treated with a phospho-specific antibody to determine the differences in the structure.

It should be noted that other types of molecules can also be phosphorylated. For example, the phosphorylation of sugars is an important part of cellular metabolism. One such example is glycolysis producing energy producing the metabolic path. The first step in the decay of glucose is the phosphorylation of the OH group on the glucose molecule.

phosphorylation of adenosine diffosphate (ADP) on ATP is necessary for many celebrations. ATP is a high -energy molecule and emits energy when donating a phosphate group. Protein synthesis is one of many important cellular processes driven, etc.