User:Elizabeth G. Aylesworth/Sandbox 1 - Revision history

Elizabeth G. Aylesworth at 18:06, 15 April 2019

Elizabeth G. Aylesworth — Mon, 15 Apr 2019 18:06:52 GMT

←Older revision		Revision as of 18:06, 15 April 2019
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	As part of the WD40-repeat protein suprafamily, coronin are expected to have at least a		As part of the WD40-repeat protein suprafamily, coronin are expected to have at least a
	repeated sequence of four WDs as well as a propeller. When the structure was determined, it		repeated sequence of four WDs as well as a propeller. When the structure was determined, it
-	was found that ~~coronin shave~~ a repeated sequence of five, and instead of a five beta-propeller,	+	was found that coronins have a repeated sequence of five, and instead of a five beta-propeller,
	it has a seven beta-propeller.		it has a seven beta-propeller.

Elizabeth G. Aylesworth at 19:19, 14 April 2019

Elizabeth G. Aylesworth — Sun, 14 Apr 2019 19:19:13 GMT

←Older revision		Revision as of 19:19, 14 April 2019
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	acids and a coiled-coil structure. Unlike the long coronin, the short coronin’s N-terminal consists		acids and a coiled-coil structure. Unlike the long coronin, the short coronin’s N-terminal consists
	twelve amino acids(11).		twelve amino acids(11).
		+
	As part of the WD40-repeat protein suprafamily, coronin are expected to have at least a		As part of the WD40-repeat protein suprafamily, coronin are expected to have at least a
	repeated sequence of four WDs as well as a propeller. When the structure was determined, it		repeated sequence of four WDs as well as a propeller. When the structure was determined, it
	was found that coronin shave a repeated sequence of five, and instead of a five beta-propeller,		was found that coronin shave a repeated sequence of five, and instead of a five beta-propeller,
	it has a seven beta-propeller.		it has a seven beta-propeller.
		+
	Three variants of coronin-1C have been identified in humans. This affects the region just before		Three variants of coronin-1C have been identified in humans. This affects the region just before
	the coiled-coil area of the coronin protein as well as the N-terminal being elongated compared to		the coiled-coil area of the coronin protein as well as the N-terminal being elongated compared to
	other coronin proteins. This protein, though complete structure has not been confirmed, does		other coronin proteins. This protein, though complete structure has not been confirmed, does
	have oligomeric properties(11).		have oligomeric properties(11).
		+
	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 (1.		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 (1.
	== Function ==		== Function ==

Elizabeth G. Aylesworth at 19:18, 14 April 2019

Elizabeth G. Aylesworth — Sun, 14 Apr 2019 19:18:44 GMT

←Older revision		Revision as of 19:18, 14 April 2019
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	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
	== History ==		== History ==
		+	Thus far, there are 723 different types of coronin proteins, and of these 723, only 614 have
		+	complete structure models. These proteins are then sorted into four types of proteins with type I
		+	and II being specific just to metazoan classes. Type III are for tandem while type IV contains
		+	coronins that fuse to villin. Along with the four types of coronin based on the organism the
		+	coronin is present in, there are also two subfamilies that consist of long coronin and short
		+	coronin. The long coronin do not have a coiled-coil structure and have two tandems in the core.
		+	The N-terminal also only has five amino acids. Short coronin has about less than 700 amino
		+	acids and a coiled-coil structure. Unlike the long coronin, the short coronin’s N-terminal consists
		+	twelve amino acids(11).
		+	As part of the WD40-repeat protein suprafamily, coronin are expected to have at least a
		+	repeated sequence of four WDs as well as a propeller. When the structure was determined, it
		+	was found that coronin shave a repeated sequence of five, and instead of a five beta-propeller,
		+	it has a seven beta-propeller.
		+	Three variants of coronin-1C have been identified in humans. This affects the region just before
		+	the coiled-coil area of the coronin protein as well as the N-terminal being elongated compared to
		+	other coronin proteins. This protein, though complete structure has not been confirmed, does
		+	have oligomeric properties(11).
	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 (1.		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 (1.
	== Function ==		== Function ==
Line 41:		Line 58:

	10. Sokolova, O., Chemeris, A., Goode, B. Structural Basis of Arp 2/3 Complex Inhibition by GMF, Coronin, and Arpin. Journal of Molecular Biology. 2017. 237-248.		10. Sokolova, O., Chemeris, A., Goode, B. Structural Basis of Arp 2/3 Complex Inhibition by GMF, Coronin, and Arpin. Journal of Molecular Biology. 2017. 237-248.
		+
		+	11. Christian Eckert, Bjorn Hammesfahr, and Martin Kollm. BMC Evol Biol. 2011; 11: 268.

Elizabeth G. Aylesworth at 14:13, 11 April 2019

Elizabeth G. Aylesworth — Thu, 11 Apr 2019 14:13:22 GMT

←Older revision		Revision as of 14:13, 11 April 2019
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	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 (1.		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 (1.
	== Function ==		== 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).	+	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. This protein "interacts with the non-alpha-helical amino-terminal domain of vimentin"(9). This helps to show how the coronin is an integrator of the filaments and microtubules. 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). Coronin 1C has a high ability to bind F-actin, which leads to depletion of the cell, lamellipodia. The amount of coronin 1C in a depleted cell is higher than any of the other coronins, which is why they believe there is a second binding site(6). Even though coronin 1C lacks a phosphorylation site, it still binds with the Arp 2/3 complex. The propeller of the coronin interacts with the open Arp 2/3 complex, which allows a conformation in shape to happen
	== Disease ==		== 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).		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).
Line 37:		Line 37:

	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.		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.
		+
		+	9. Behrens J., Solga R., et all. Coronin 1C-free primary mouse fibroblasts exhibit robust rearrangements in the orientation of actin filamnets, microtublues and intermediate filaments. European Journal of Cell Biology. 2016. 8. 239-251.
		+
		+	10. Sokolova, O., Chemeris, A., Goode, B. Structural Basis of Arp 2/3 Complex Inhibition by GMF, Coronin, and Arpin. Journal of Molecular Biology. 2017. 237-248.

Elizabeth G. Aylesworth at 13:11, 11 April 2019

Elizabeth G. Aylesworth — Thu, 11 Apr 2019 13:11:08 GMT

←Older revision		Revision as of 13:11, 11 April 2019
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	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
	== History ==		== 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 ~~<ref>~~(1~~)<ref>~~.	+	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 (1.
	== Function ==		== 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).		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).

Elizabeth G. Aylesworth at 13:10, 11 April 2019

Elizabeth G. Aylesworth — Thu, 11 Apr 2019 13:10:25 GMT

←Older revision		Revision as of 13:10, 11 April 2019
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	==Coronin 1C==		==Coronin 1C==
	<StructureSection load='2AQ5' size='340' side='right' caption='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.' scene=''>		<StructureSection load='2AQ5' size='340' side='right' caption='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.' scene=''>
-	~~This is a default text for your page '''Elizabeth G. Aylesworth/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.~~	+
	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
	== History ==		== 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 (1).	+	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 <ref>(1)<ref>.
	== Function ==		== 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).		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).

Elizabeth G. Aylesworth at 20:08, 10 April 2019

Elizabeth G. Aylesworth — Wed, 10 Apr 2019 20:08:16 GMT

←Older revision		Revision as of 20:08, 10 April 2019
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	<references/>		<references/>
	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.		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		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/		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		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		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.		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.		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.		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.

Elizabeth G. Aylesworth at 20:07, 10 April 2019

Elizabeth G. Aylesworth — Wed, 10 Apr 2019 20:07:36 GMT

←Older revision		Revision as of 20:07, 10 April 2019
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	== Structural highlights ==		== 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).		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).		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).

Line 21:		Line 22:
	== References ==		== References ==
	<references/>		<references/>
		+	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.

Elizabeth G. Aylesworth at 20:06, 10 April 2019

Elizabeth G. Aylesworth — Wed, 10 Apr 2019 20:06:39 GMT

←Older revision		Revision as of 20:06, 10 April 2019
Line 4:		Line 4:
	This is a default text for your page '''Elizabeth G. Aylesworth/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Elizabeth G. Aylesworth/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.		You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> 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 (1).
	== Function ==		== 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 ==		== 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 ==		== 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 ==		== 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.		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.

Elizabeth G. Aylesworth at 21:01, 9 April 2019

Elizabeth G. Aylesworth — Tue, 09 Apr 2019 21:01:19 GMT

←Older revision		Revision as of 21:01, 9 April 2019
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	Coronin		Coronin
-	==~~Your Heading Here (maybe something like 'Structure')~~==	+	==Coronin 1C==
	<StructureSection load='2AQ5' size='340' side='right' caption='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.' scene=''>		<StructureSection load='2AQ5' size='340' side='right' caption='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.' scene=''>
	This is a default text for your page '''Elizabeth G. Aylesworth/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Elizabeth G. Aylesworth/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.