User:Elizabeth G. Aylesworth/Sandbox 1

From Proteopedia

proteopedia linkproteopedia link

Coronin

Coronin 1C

spinqualitylabelsall models Above is a diagram of Coronin 1. The reason coronin 1C is not pictured is because there is not a code for that specific protein. Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. History Dictyostelium discoideum was the first organism in which coronin was identified. Since that discovery in 1991, plants are the only eukaryotes that coronin has not been identified. There are 12 subfamilies, and half of them are found only in vertebrates [3]

References

1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
3. ↑ (1)<ref>. == Function == The function of coronin 1C can be seen in many parts of the cell. Coronin 1C helps the cell to migrate by “regulation the activation and subcellular location of RAC1” (2). Coronin 1C helps to organize the cytoskeleton, helps the proliferation of the cell, and helps form a lamellipodia. Coronin 1C is “localized to endosome membrane tubules and promotes recruitment of TMCC1, leading to recruitment of the endoplasmic reticulum to endosome tubules for fission” (2). == Disease == Coronin 1C is seen in many different cancers. The promotor of coronin 1C binds to C-myc in lymphoma cells. The levels of coronin 1C are low in normal skin cells, but high in melanoma cells. It is used as a marker for hepatocellular carcinoma (HCC), but the expression is dependent on the Erk pathway. If coronin 1C is imbalanced, it could lead to a defect in the brain growth. This could also lead to brain diseases. Coronin 1C is high at the start of development and decreases as the brain develops. Coronin 1C is also found in brain tumors, but the levels depend on where the brain tumor is in the brain (3). == Relevance == Coronin 1C uses the Arp 2/3 complex with motility and phagocytosis. A deletion of the gene coding for coronin does not cause abnormal function of endocytosis, but it does interact abnormally with other genetic mutations. For this reason, coronin is an important protein for the proper function and form of the cytoskeleton. In other organisms coronin being either deleted completely or over or under produced can prove to affect endocytosis and phagocytosis negatively or be deadly (4). == Structural highlights == Coronin 1C is a part of proteins that are approximately 474 amino acids long. Coronin 1A has Asp452 on the 3 position, whereas Coronin 1C has Ser463. This allows the protein to be phosphorylated, which interferes with Arg461’-Glu466, thus leading to the loss of a coil. Another structural difference is that Coronin 1C has a Ser450 in a hexa-peptide, which is not found in other coronin proteins. This allows for another phosphorylation site for the protein. This, however, has not been shown to impact the protein function in significant ways (5). There are three parts of coronin 1C: the propeller, unique segment, and coiled coil domain. The propeller binds with the F-actin. The coiled coil domain helps coronin 1C bind with Arp 2/3 complex and forms trimers and dimers. The unique segment is not fully understood. Coronin 1C is different because it also has a second actin binding site. Coronin 1C lacks the phosphorylation site but can still bind the complex (6). If the Coronin 1C is phosphorylated, then the protein moves throughout the cytoplasm, not reacting with the plasma membrane. Coronin 1C is eight residues longer than 1A. If the coiled coil domain is deleted in coronin 1C, it prevents the creation of a bond to the plasma membrane (7). It is not a transmembrane protein and instead only binds to the membrane with the cytoskeleton through interaction with cholesterol (8). This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. </li></ol></ref>

1. Clemen C.S., Rybakin V., Eichinger L. (2008) The Coronin Family of Proteins. In: Clemen C.S., Eichinger L., Rybakin V. (eds) The Coronin Family of Proteins. Subcellular Biochemistry, vol 48. Springer, New York, NY.

2. Uniport. COR1C_MOUSE. 2019. https://www.uniprot.org/uniprot/Q9WUM4

3. Roadcap DW.; Clemen CS.; Bear, JE. Madame Curie Bioscience Database. The Role of Mammalian Coronins in Development and Disease. 2013. https://www.ncbi.nlm.nih.gov/books/NBK6528/

4. Meghal Gandhi and Bruce L Goode. Coronin: The Double-Edged Sword of Actin Dynamics. In: Madame Curie Bioscience Database [Internet]. Landes Bioscience; 2000-2013

5. McArdle B, Hofmann A. Coronin Structure and Implications. In: Madame Curie Bioscience Database [Internet]. Landes Bioscience; 2000-2013

6. Chan, K., Roadcap, D., Holoweckyj, N., Bear, J., Biochemical Journal. Coronin 1C harbours a second actin biding site that confers co-operative binding to F-Actin. 2012. 444. 89-96.

7. Long Wu, Chun-Wei Peng et. al. Journal of Experimental and Clinical Cancer Research; 29:17. BioMed Central, 24 February 2010.

8. Tokarz-Deptula, B.; Malinowska, M.; Adamiak, M.; Deptula, W. Coronins and their role in immunological phenomena. Central European Journal of Immunology 2017 DOI: 10.3897/bdj.4.e7720.figure2f.