What Is The ER Quality Control Process?

The endoplasmic reticulum is specialised for protein processing and lipid biosynthesis. One of its primary functions is to regulate the ionic concentration in the cytoplasm via the movement of Ca2+, via ionic pumps and channels. It also contains enzymes responsible for the metabolising of drugs. Endoplasmic reticulum (ER) can come in two forms. As depicted in Fig. 2 Rough ER has ribosomes present as part of the membrane of the organelle, and together with these ribosomes takes polypeptides and amino acids from the cytosol and synthesises proteins destined for attachment to cell membranes. It is in the lumen of the rough ER that the proteins are folded into the specific three dimensional shapes that are so important for biochemical recognition and linking sites [6]. It is called rough because of the presence of ribosomes makes the surface of the membrane look rough, unlike smooth ER, which lacks the ribosomes so the membrane looks smooth. Rough ER is composed of a large but convoluted flattened sac. The main function of the smooth ER is the production of lipids and the metabolism of compounds (such as the breakdown of glycogen into glucose). Because of the different functions between the rough and smooth ER, different specialised cells will have different amounts of each; for example, hepatic

One of the main manufacturing facilities within a cell. Consists of rough ER and smooth ER, they are physically connected but differ in structure. Consist of membrane-enclosed tubes and sacs within the cytoplasm. Rough ER, named for the ribosomes attached to its surface, make membrane and secretory proteins. One function of rough ER is to produce new membrane. Some products by rough ER are dispatched to other locations by transport vesicles.

Endoplasmic reticulum (ER) – Endoplasmic reticulum is a branching network that fills the cell interior. There two types of ER: Smooth endoplasmic reticulum (SER) – Synthesis of lipid, glycogen and steroids (e.g. cholesterol and testosterone).

There are two types of Endoplasmic Reticulum the Smooth ER and the Rough ER. you can distinguish that both of the ER’s are different to each other, this is shown in the diagram above that one is smooth ER and the other is rough ER the rough ER has ribsomes attracted to it while the smooth ER does not have ribosomes attached to it. The two ER’s have different function to each other.

The body has two faces, the cis face which fuses with incoming transport vesicles, and the trans face which excretes the secretory vesicles. The cis face fuses with vesicles coming from the ER effectively from many directions due to its convex shape, whereas the concave trans face can direct the secretory vesicles to their destination. When fusing with the cis face, the transport vesicles release their proteins to be absorbed for modification. Each cisternal layer of the Golgi body holds different enzymes which each modify the passing proteins in separate ways. Between the layers the proteins are moved through the gaps by small vesicles. When a protein has been modified correctly, it leaves the Golgi body via secretory vesicles which then carry the modified proteins to the cell membrane or another organelle. The proteins that are transported to the cell membrane are either excreted from the cell, or absorbed into the membrane to aid with its function. Some of the secretory vesicles which hold hydrolytic enzymes stay within the cytoplasm and function as lysosomes.

Proteins are the metabolic workhorses of the cell; they engage in a variety of essential activities ranging from enzymatically catabolizing macromolecular food sources to serving as structural components that maintain cell stability. Maximizing protein function relies on intricate non-covalent interactions occurring on the secondary, tertiary, and quaternary levels that help determine the overall shape of the protein. In their native states, proteins will assume the most energetically favorable configuration. Occasionally however, cells are exposed to exogenous disruptions such as heat stress. Heat Stress can compromise protein three-dimensional structure. Hydrophobic residues tend to be buried in the interior of the protein but when

The chaperones have the main role of ensuring proper folding. When a chaperone protein becomes toxic, major changes in the conformation occur as the alpha helix becomes beta pleated sheets. The sheets now expose the hydrophobic amino acid and aggregation, or clumping together of sheets occurs (Borges, 2014).

is loss of its structure. This occurs when the ionics and hydrogens bonds of the protein

Since we have already known the amino sequence of the protein in previous step, we can narrow down the targeting ubiquitin ligase based on existing research data such as papers, NCBI data.

Proteins are primarily considered to have one primary function to serve its role in an organism, however studies have observed to have multiple functioning proteins known as moonlighting proteins (Khan et al. 2014). Moonlighting proteins along with primary functions, have secondary functions that are not related to the primary function and does not correlate to the primary or other functions (Khan et al. 2014). The multifunctional proteins play essential roles in carrying out biochemical functions which aids in the cell growth but are not caused by gene fusion and multiple RNA splice variants (Amblee et al. 2015). The discovery of moonlighting proteins was first discovered by Piatigorsky and Wistow while observing crystallins (Khan et al. 2014). Crystallins, are structural proteins that are found in the eye lens that exhibit enzymatic activity to make the lens itself (Khan et al. 2014). Crystallin has a primary function to help form the lens of the eye by acting as a structural protein (Amblee et al. 2015). Besides enzymatic activity, crystallin was observed in other mammals to have secondary functions such as metabolic functions which are helpful in prokaryotic (Khan et al 2014). Most moonlighting proteins are characterized as cytosolic enzymes and chaperons, or in other words helping proteins (Amblee et al 2015). The multifunctional proteins or moonlighting proteins can also be identified as receptors, channel proteins and ribosomal proteins (Khan et al. 2014). Due to the

These proteins differ depending on their function in the cell, but often prevent misfolding of nascent protein, and assist in refolding of the misfolded proteins. Protein folding is dependent on the amino acid sequence within the polypeptide chain that is synthesized from the DNA strand in the ribosome.2 Upon release from the ribosome, the polypeptide chain undergoes a series of conformational changes based on the amino acid sequence to produce a functional protein structure. The assembled native protein is directed to the ER via vesicle

For the second part of the experiment, one had to use the knowledge learn from viewing protein molecules in FirstGlance in Jmol to analyze the protein PDB ID: 4EEY. The analysis of this protein was done using the RSCB protein data bank (PDB) at (http://www.rcsb.org/pdb/home/home.do).2

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

The endoplasmic reticulum (ER) is an essential organelle that is a major place for the biogenesis of cellular components including proteins, lipids, and carbohydrates and internal calcium storage. ER is primarily responsible for protein translocation, protein folding and protein post modification. Proper folding of protein in the ER is accomplished with the aid of ER resident proteins or enzymes such as chaperones. Binding of chaperones to

Molecular chaperones stabilize unfolded or misfolded proteins until native conformations have been obtained to promote cell survival during and after stress conditions. They do not change or add to the folding principles encoded by a protein because polypeptide chains inherently carry within them all the information that is necessary for achieving the native state of a protein. Instead, they optimize the folding process by stabilizing folding intermediates and are involved in every aspect of proteome maintenance including de novo folding, refolding of stress-induced misfolded proteins, and targeting proteins for degradation (Hartl 2009, Hartl 2011). Chaperones, many of which are induced or upregulated only during stress conditions, work in cooperative networks when protein-aggregate concentration