Related Research Articles
The endomembrane system is composed of the different membranes (endomembranes) that are suspended in the cytoplasm within a eukaryotic cell. These membranes divide the cell into functional and structural compartments, or organelles. In eukaryotes the organelles of the endomembrane system include: the nuclear membrane, the endoplasmic reticulum, the Golgi apparatus, lysosomes, vesicles, endosomes, and plasma (cell) membrane among others. The system is defined more accurately as the set of membranes that forms a single functional and developmental unit, either being connected directly, or exchanging material through vesicle transport. Importantly, the endomembrane system does not include the membranes of plastids or mitochondria, but might have evolved partially from the actions of the latter.
The Golgi apparatus, also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. Part of the endomembrane system in the cytoplasm, it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus.
Cux1 is a homeodomain protein that in humans is encoded by the CUX1 gene.
General vesicular transport factor p115 is a protein that in humans is encoded by the USO1 gene.
Syntaxin-5 is a protein that in humans is encoded by the STX5 gene.
Golgi SNAP receptor complex member 1 is a protein that in humans is encoded by the GOSR1 gene.
Golgi reassembly-stacking protein of 55 kDa (GRASP55) also known as golgi reassembly-stacking protein 2 (GORASP2) is a protein that in humans is encoded by the GORASP2 gene. It was identified by its homology with GRASP65 and the protein's amino acid sequence was determined by analysis of a molecular clone of its complementary DNA. The first (N-terminus) 212 amino acid residues of GRASP55 are highly homologous to those of GRASP65, but the remainder of the 454 amino acid residues are highly diverged from GRASP65. The conserved region is known as the GRASP domain, and it is conserved among GRASPs of a wide variety of eukaryotes, but not plants. The C-terminus portion of the molecule is called the SPR domain. GRASP55 is more closely related to homologues in other species, suggesting that GRASP55 is ancestral to GRASP65. GRASP55 is found associated with the medial and trans cisternae of the Golgi apparatus.
Conserved oligomeric Golgi complex subunit 3 is a protein that in humans is encoded by the COG3 gene.
Conserved oligomeric Golgi complex subunit 7 is a protein that in humans is encoded by the COG7 gene.
Golgin subfamily A member 5 is a protein that in humans is encoded by the GOLGA5 gene.
Conserved oligomeric Golgi complex subunit 4 is a protein that in humans is encoded by the COG4 gene.
Alpha-mannosidase 2 is an enzyme that in humans is encoded by the MAN2A1 gene.
Conserved oligomeric Golgi complex subunit 8 is a protein that in humans is encoded by the COG8 gene.
Conserved oligomeric Golgi complex subunit 5 is a protein that in humans is encoded by the COG5 gene.
Conserved oligomeric Golgi complex subunit 1 is a protein that in humans is encoded by the COG1 gene.
Conserved oligomeric Golgi complex subunit 2 is a protein that in humans is encoded by the COG2 gene.
Vesicle transport protein GOT1B is a protein that in humans is encoded by the GOLT1B gene.
N-linked glycosylation, is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom, in a process called N-glycosylation, studied in biochemistry. The resulting protein is called an N-linked glycan, or simply an N-glycan.
Wrinkly skin syndrome(WSS) is a rare genetic condition characterized by sagging, wrinkled skin, low skin elasticity, and delayed fontanelle (soft spot) closure, along with a range of other symptoms. The disorder exhibits an autosomal recessive inheritance pattern with mutations in the ATP6V0A2 gene, leading to abnormal glycosylation events. There are only about 30 known cases of WSS as of 2010. Given its rarity and symptom overlap with other dermatological conditions, reaching an accurate diagnosis is difficult and requires specialized dermatological testing. Limited treatment options are available but long-term prognosis is variable from patient to patient, based on individual case studies. Some skin symptoms recede with increasing age, while progressive neurological advancement of the disorder causes seizures and mental deterioration later in life for some patients.
O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the cytoplasm; in prokaryotes, it occurs in the cytoplasm. Several different sugars can be added to the serine or threonine, and they affect the protein in different ways by changing protein stability and regulating protein activity. O-glycans, which are the sugars added to the serine or threonine, have numerous functions throughout the body, including trafficking of cells in the immune system, allowing recognition of foreign material, controlling cell metabolism and providing cartilage and tendon flexibility. Because of the many functions they have, changes in O-glycosylation are important in many diseases including cancer, diabetes and Alzheimer's. O-glycosylation occurs in all domains of life, including eukaryotes, archaea and a number of pathogenic bacteria including Burkholderia cenocepacia, Neisseria gonorrhoeae and Acinetobacter baumannii.
References
- 1 2 Ungar D, Oka T, Brittle EE, Vasile E, Lupashin VV, Chatterton JE, Heuser JE, Krieger M, Waters MG (Apr 2002). "Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function". J Cell Biol. 157 (3): 405–15. doi:10.1083/jcb.200202016. PMC 2173297 . PMID 11980916.
- ↑ "Entrez Gene: COG5 component of oligomeric golgi complex 5".
- ↑ Ungar et al., 2002)
- ↑ Smith RD, Lupashin VV (2008). "Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation". Carbohydr Res. 343 (12): 2024–31. doi:10.1016/j.carres.2008.01.034. PMC 2773262 . PMID 18353293.
