Group:MUZIC:FilaminC - Revision history

Jaime Prilusky at 11:33, 1 July 2015

Jaime Prilusky — Wed, 01 Jul 2015 11:33:14 GMT

←Older revision		Revision as of 11:33, 1 July 2015
Line 105:		Line 105:
	== '''References''' ==		== '''References''' ==
	<references />		<references />
		+	[[Category: Z-disk]]

Nikos Pinotsis: /* '''Sequence''' */

Nikos Pinotsis — Tue, 02 Apr 2013 11:03:40 GMT

'''Sequence'''

←Older revision		Revision as of 11:03, 2 April 2013
Line 1:		Line 1:
-		+	{{TOC limit\|limit=3}}
-	{{TOC limit\|limit=3}}	+


Line 16:		Line 15:
	== '''Sequence''' ==		== '''Sequence''' ==

-	[http://www.uniprot.org/uniprot/q14315 ~~Amino acid sequence of Human Filamin C] is available from~~ uniprot. The sequence annotation based on the tertiary structure is provided in Figure 1. Note that in Filamin C, Hinge 1 is absent. Also, the evidence for the presence of domain pairs in the C terminal region is only confirmed for FLNa and FLNb. <ref> PMID 19699211 </ref> <ref> PMID 19622754 </ref> <ref> PMID 21636571 </ref>	+	The amino-acid sequence of Human Filamin C is available from uniprot [http://www.uniprot.org/uniprot/q14315 uniprot]. The sequence annotation based on the tertiary structure is provided in Figure 1. Note that in Filamin C, Hinge 1 is absent. Also, the evidence for the presence of domain pairs in the C terminal region is only confirmed for FLNa and FLNb. <ref> PMID 19699211 </ref> <ref> PMID 19622754 </ref> <ref> PMID 21636571 </ref>

	== '''3D Structures''' ==		== '''3D Structures''' ==

Ritika Sethi at 10:06, 8 February 2013

Ritika Sethi — Fri, 08 Feb 2013 10:06:57 GMT

←Older revision		Revision as of 10:06, 8 February 2013
Line 72:		Line 72:
	• Integrin β1A - Domain 19-24 <ref> PMID 16076904 </ref>		• Integrin β1A - Domain 19-24 <ref> PMID 16076904 </ref>

-	• Migfilin - Domain 21 <ref> PMID 18829455 </ref>	+	• Migfilin - Domain 21 <ref> PMID 18829455 </ref> <ref> PMID 19074766 </ref>

	• [[Group:MUZIC:Myotilin\|Myotilin]] - Domain 19-21 <ref name="Van der" />		• [[Group:MUZIC:Myotilin\|Myotilin]] - Domain 19-21 <ref name="Van der" />

-	• FATZ-1 (myozenin-1, calsarcin 2) - Domain 20-24<ref> PMID 16076904 </ref>	+	• FATZ-1 (myozenin-1, calsarcin 2) - Domain 20-24 <ref> PMID 16076904 </ref>

	• [[Group:MUZIC:Xin \|Xin ]] - Domain 20 <ref> PMID 16631741 </ref>		• [[Group:MUZIC:Xin \|Xin ]] - Domain 20 <ref> PMID 16631741 </ref>

Ritika Sethi at 10:01, 8 February 2013

Ritika Sethi — Fri, 08 Feb 2013 10:01:13 GMT

←Older revision		Revision as of 10:01, 8 February 2013
Line 106:		Line 106:
	== '''References''' ==		== '''References''' ==
	<references />		<references />
-
-	<ref group="xtra">PMID:21524097</ref><ref group="xtra">PMID:16416311</ref><ref group="xtra">PMID:19830582</ref><ref group="xtra">PMID:18056414</ref><ref group="xtra">PMID:21169733</ref><ref group="xtra">PMID:19622754</ref><ref group="xtra">PMID:19050726 </ref><ref group="xtra">PMID:11252955</ref><ref group="xtra">PMID:9501083 </ref><references group="xtra"/>

Ritika Sethi at 09:24, 23 November 2012

Ritika Sethi — Fri, 23 Nov 2012 09:24:23 GMT

←Older revision		Revision as of 09:24, 23 November 2012
Line 16:		Line 16:
	== '''Sequence''' ==		== '''Sequence''' ==

-	[http://www.uniprot.org/uniprot/q14315 Amino acid sequence of Human Filamin C] is available from uniprot. The sequence annotation based on the tertiary structure is provided in Figure 1. Note that in Filamin C, Hinge 1 is absent.	+	[http://www.uniprot.org/uniprot/q14315 Amino acid sequence of Human Filamin C] is available from uniprot. The sequence annotation based on the tertiary structure is provided in Figure 1. Note that in Filamin C, Hinge 1 is absent. Also, the evidence for the presence of domain pairs in the C terminal region is only confirmed for FLNa and FLNb. <ref> PMID 19699211 </ref> <ref> PMID 19622754 </ref> <ref> PMID 21636571 </ref>

	== '''3D Structures''' ==		== '''3D Structures''' ==

Ritika Sethi at 09:19, 23 November 2012

Ritika Sethi — Fri, 23 Nov 2012 09:19:12 GMT

←Older revision		Revision as of 09:19, 23 November 2012
Line 9:		Line 9:
	In humans, 3 isoforms of Filamins exist that are coded by 3 different genes. While the genes for [[Filamin A]] and [[Filamin B]] are present on the X chromosome and chromosome 3 respectively, and both show a ubiquitous expression in many tissues, gene for Filamin C is located on the Chromosome 7 and the encoded protein is specifically expressed in muscles and has been predicted to have a Z disc targeting motif. <ref name="Van der"> PMID 11038172 </ref>		In humans, 3 isoforms of Filamins exist that are coded by 3 different genes. While the genes for [[Filamin A]] and [[Filamin B]] are present on the X chromosome and chromosome 3 respectively, and both show a ubiquitous expression in many tissues, gene for Filamin C is located on the Chromosome 7 and the encoded protein is specifically expressed in muscles and has been predicted to have a Z disc targeting motif. <ref name="Van der"> PMID 11038172 </ref>

-	Filamin C (also known as FLNc/Gamma-Filamin/ ABPL) is an actin binding homodimeric protein composed of two 290 kDa subunits. Each subunit is composed of an α-actinin like N terminal actin binding domain (ABD) made up of 2 calponin homology tandem repeats followed by a flexible rod region containing 24 Immunoglobulin like domains (Ig- like) of around 96 residues each. The most C terminal domain (Ig 24) is the self association domain required for its dimerization ability. (Shown on right) The presence of 2 flexible calpain sensitive hinges, Hinge 1 between domain 15 and 16 divides the subunit into Rod 1 and Rod 2 domains and Hinge 2 between 23 and 24 separates the dimerization domain from the rest of domains. ~~Each Ig domain is made of 7 β strands arranged antiparallel in group of 4 and 3 sheets forming a β sandwich.~~ It is noteworthy to mention that the Hinge 1 is alternatively spliced and the majorly expressed variant of FLNc in striated muscles, lacks this hinge <ref> PMID 9791010 </ref>.	+	Filamin C (also known as FLNc/Gamma-Filamin/ ABPL) is an actin binding homodimeric protein composed of two 290 kDa subunits. Each subunit is composed of an α-actinin like N terminal actin binding domain (ABD) made up of 2 calponin homology tandem repeats followed by a flexible rod region containing 24 Immunoglobulin like domains (Ig- like) of around 96 residues each. Each Ig domain is made of 7 β strands arranged antiparallel in group of 4 and 3 sheets forming a β sandwich. The most C terminal domain (Ig 24) is the self association domain required for its dimerization ability. (Shown on right) The presence of 2 flexible calpain sensitive hinges, Hinge 1 between domain 15 and 16 divides the subunit into Rod 1 and Rod 2 domains and Hinge 2 between 23 and 24 separates the dimerization domain from the rest of domains. It is noteworthy to mention that the Hinge 1 is alternatively spliced and the majorly expressed variant of FLNc in striated muscles, lacks this hinge <ref> PMID 9791010 </ref>. Also, in FLNc, there is a unique insertion of 80 amino acid residues in domain 20, which is predicted to play a role in Z disc targeting. <ref> PMID 16631741 </ref>
	As the three Filamin proteins share around 70% homology over the entire sequence with the exception of the hinges <ref name="Flier"> PMID 11336782 </ref>, not many structures of the Filamin C domains exist in the PDB.		As the three Filamin proteins share around 70% homology over the entire sequence with the exception of the hinges <ref name="Flier"> PMID 11336782 </ref>, not many structures of the Filamin C domains exist in the PDB.

Ritika Sethi at 09:12, 23 November 2012

Ritika Sethi — Fri, 23 Nov 2012 09:12:27 GMT

←Older revision		Revision as of 09:12, 23 November 2012
Line 68:		Line 68:


-	Some of the major interacting partners are shown in the diagram here.	+	Some of the major interacting partners are shown in the diagram here. <ref> PMID 23109048 </ref>

	• Integrin β1A - Domain 19-24 <ref> PMID 16076904 </ref>		• Integrin β1A - Domain 19-24 <ref> PMID 16076904 </ref>

Ritika Sethi at 09:11, 23 November 2012

Ritika Sethi — Fri, 23 Nov 2012 09:11:22 GMT

←Older revision		Revision as of 09:11, 23 November 2012
Line 100:		Line 100:
	• A mutation of 577G---->A (Ala193Thr)in the Filamin C ABD has been shown to cause dominant distal myopathy <ref> PMID 21620354 </ref>		• A mutation of 577G---->A (Ala193Thr)in the Filamin C ABD has been shown to cause dominant distal myopathy <ref> PMID 21620354 </ref>

-	For an extended pathophysiology of the MFM, see <ref> PMID 22961544 </ref>	+	For an extended pathophysiology of the MFM, see <ref> PMID 22961544 </ref> <ref> PMID 23109048 </ref>

Ritika Sethi at 08:56, 23 November 2012

Ritika Sethi — Fri, 23 Nov 2012 08:56:01 GMT

←Older revision		Revision as of 08:56, 23 November 2012
Line 9:		Line 9:
	In humans, 3 isoforms of Filamins exist that are coded by 3 different genes. While the genes for [[Filamin A]] and [[Filamin B]] are present on the X chromosome and chromosome 3 respectively, and both show a ubiquitous expression in many tissues, gene for Filamin C is located on the Chromosome 7 and the encoded protein is specifically expressed in muscles and has been predicted to have a Z disc targeting motif. <ref name="Van der"> PMID 11038172 </ref>		In humans, 3 isoforms of Filamins exist that are coded by 3 different genes. While the genes for [[Filamin A]] and [[Filamin B]] are present on the X chromosome and chromosome 3 respectively, and both show a ubiquitous expression in many tissues, gene for Filamin C is located on the Chromosome 7 and the encoded protein is specifically expressed in muscles and has been predicted to have a Z disc targeting motif. <ref name="Van der"> PMID 11038172 </ref>

-	Filamin C (also known as FLNc/Gamma-Filamin/ ABPL) is an actin binding homodimeric protein composed of two 290 kDa subunits. Each subunit is composed of an α-actinin like N terminal actin binding domain (ABD) made up of 2 calponin homology tandem repeats followed by a flexible rod region containing 24 Immunoglobulin like domains (Ig- like) of around 96 residues each. The most C terminal domain (Ig 24) is the self association domain required for its dimerization ability. (Shown on right) The presence of 2 flexible calpain sensitive hinges, Hinge 1 between domain 15 and 16 divides the subunit into Rod 1 and Rod 2 domains and Hinge 2 between 23 and 24 separates the dimerization domain from the rest of domains. Each Ig domain is made of 7 β strands arranged antiparallel in group of 4 and 3 sheets forming a β sandwich. It is noteworthy to mention that the Hinge 1 is alternatively spliced and the majorly expressed variant of FLNc in striated muscles, lacks this hinge.	+	Filamin C (also known as FLNc/Gamma-Filamin/ ABPL) is an actin binding homodimeric protein composed of two 290 kDa subunits. Each subunit is composed of an α-actinin like N terminal actin binding domain (ABD) made up of 2 calponin homology tandem repeats followed by a flexible rod region containing 24 Immunoglobulin like domains (Ig- like) of around 96 residues each. The most C terminal domain (Ig 24) is the self association domain required for its dimerization ability. (Shown on right) The presence of 2 flexible calpain sensitive hinges, Hinge 1 between domain 15 and 16 divides the subunit into Rod 1 and Rod 2 domains and Hinge 2 between 23 and 24 separates the dimerization domain from the rest of domains. Each Ig domain is made of 7 β strands arranged antiparallel in group of 4 and 3 sheets forming a β sandwich. It is noteworthy to mention that the Hinge 1 is alternatively spliced and the majorly expressed variant of FLNc in striated muscles, lacks this hinge <ref> PMID 9791010 </ref>.
	As the three Filamin proteins share around 70% homology over the entire sequence with the exception of the hinges <ref name="Flier"> PMID 11336782 </ref>, not many structures of the Filamin C domains exist in the PDB.		As the three Filamin proteins share around 70% homology over the entire sequence with the exception of the hinges <ref name="Flier"> PMID 11336782 </ref>, not many structures of the Filamin C domains exist in the PDB.

Ritika Sethi at 08:53, 23 November 2012

Ritika Sethi — Fri, 23 Nov 2012 08:53:28 GMT

←Older revision		Revision as of 08:53, 23 November 2012
Line 9:		Line 9:
	In humans, 3 isoforms of Filamins exist that are coded by 3 different genes. While the genes for [[Filamin A]] and [[Filamin B]] are present on the X chromosome and chromosome 3 respectively, and both show a ubiquitous expression in many tissues, gene for Filamin C is located on the Chromosome 7 and the encoded protein is specifically expressed in muscles and has been predicted to have a Z disc targeting motif. <ref name="Van der"> PMID 11038172 </ref>		In humans, 3 isoforms of Filamins exist that are coded by 3 different genes. While the genes for [[Filamin A]] and [[Filamin B]] are present on the X chromosome and chromosome 3 respectively, and both show a ubiquitous expression in many tissues, gene for Filamin C is located on the Chromosome 7 and the encoded protein is specifically expressed in muscles and has been predicted to have a Z disc targeting motif. <ref name="Van der"> PMID 11038172 </ref>

-	Filamin C is an actin binding homodimeric protein composed of two 290 kDa subunits. Each subunit is composed of an α actinin like N terminal actin binding domain (ABD) made up of 2 calponin homology tandem repeats followed by a flexible rod region containing 24 Immunoglobulin like domains (Ig- like) of around 96 residues each. The most C terminal domain (Ig 24) is the self association domain required for its dimerization ability. (Shown on right) The presence of 2 flexible calpain sensitive hinges, Hinge 1 between domain 15 and 16 divides the subunit into Rod 1 and Rod 2 domains and Hinge 2 between 23 and 24 separates the dimerization domain from the rest of domains. Each Ig domain is made of 7 β strands arranged antiparallel in group of 4 and 3 sheets forming a β sandwich.	+	Filamin C (also known as FLNc/Gamma-Filamin/ ABPL) is an actin binding homodimeric protein composed of two 290 kDa subunits. Each subunit is composed of an α-actinin like N terminal actin binding domain (ABD) made up of 2 calponin homology tandem repeats followed by a flexible rod region containing 24 Immunoglobulin like domains (Ig- like) of around 96 residues each. The most C terminal domain (Ig 24) is the self association domain required for its dimerization ability. (Shown on right) The presence of 2 flexible calpain sensitive hinges, Hinge 1 between domain 15 and 16 divides the subunit into Rod 1 and Rod 2 domains and Hinge 2 between 23 and 24 separates the dimerization domain from the rest of domains. Each Ig domain is made of 7 β strands arranged antiparallel in group of 4 and 3 sheets forming a β sandwich. It is noteworthy to mention that the Hinge 1 is alternatively spliced and the majorly expressed variant of FLNc in striated muscles, lacks this hinge.
	As the three Filamin proteins share around 70% homology over the entire sequence with the exception of the hinges <ref name="Flier"> PMID 11336782 </ref>, not many structures of the Filamin C domains exist in the PDB.		As the three Filamin proteins share around 70% homology over the entire sequence with the exception of the hinges <ref name="Flier"> PMID 11336782 </ref>, not many structures of the Filamin C domains exist in the PDB.

Line 82:		Line 82:
	• Gamma- and delta-sarcoglycans - Domain 23-24 <ref> PMID 10629222 </ref>		• Gamma- and delta-sarcoglycans - Domain 23-24 <ref> PMID 10629222 </ref>

-	• [[Group:MUZIC:Myopodin\|Myopodin]] - Domain 19-21 <ref> PMID 20554076 </ref> ~~(Interaction shown in Figure 2)~~	+	• [[Group:MUZIC:Myopodin\|Myopodin]] - Domain 19-21 <ref> PMID 20554076 </ref>