Group:MUZIC:Plectin - Revision history

Jaime Prilusky at 11:31, 1 July 2015

2015-07-01T11:31:28Z

←Older revision		Revision as of 11:31, 1 July 2015
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	<references/>		<references/>
		+	[[Category: Z-disk]]

Michal Harel at 09:03, 20 February 2014

2014-02-20T09:03:47Z

←Older revision		Revision as of 09:03, 20 February 2014
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-	<StructureSection load='3pe0' size='450' side='right' scene='User:Jae-Geun_Song/Workbench/plectin/Plakin/1' caption=''>	+	<StructureSection load='3pe0' size='450' side='right' scene='User:Jae-Geun_Song/Workbench/plectin/Plakin/1' caption='Human plectin plakin domain (PDB code [[3pe0]])'>

	== Introduction ==		== Introduction ==
-	Plectin is a multidomain protein with large size (>500kDa) and versatile binding properties, which abundantly expressed in a wide variety of mammalian tissues and cell types, combined with different binding partners. It has important functions in maintaining the mechanical stability of skin, skeletal muscle and heart.	+	'''Plectin''' is a multidomain protein with large size (>500kDa) and versatile binding properties, which abundantly expressed in a wide variety of mammalian tissues and cell types, combined with different binding partners. It has important functions in maintaining the mechanical stability of skin, skeletal muscle and heart.

	The plectin gene has unusual 5'-end diversity, which is alternatively spliced into exon 2 and makes 11 kinds of isoforms.		The plectin gene has unusual 5'-end diversity, which is alternatively spliced into exon 2 and makes 11 kinds of isoforms.

Alexander Berchansky at 10:43, 8 May 2013

2013-05-08T10:43:58Z

←Older revision		Revision as of 10:43, 8 May 2013
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	The isoform-1 of the human plectin contains 4,684 amino acids [http://www.uniprot.org/uniprot/Q15149 (uniprot:Q15149)]. Plectin can be divided in three main sections; a central coiled-coil rod domain(exon 31), N and C-terminal globular region and exhibits a dumbbell like structure <ref>PMID:8633055</ref>. C-terminal region (exon 32) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (exon 2-8) and <scene name='User:Jae-Geun_Song/Workbench/plectin/Plakin/1'>plakin domain</scene> (exon 9-30).		The isoform-1 of the human plectin contains 4,684 amino acids [http://www.uniprot.org/uniprot/Q15149 (uniprot:Q15149)]. Plectin can be divided in three main sections; a central coiled-coil rod domain(exon 31), N and C-terminal globular region and exhibits a dumbbell like structure <ref>PMID:8633055</ref>. C-terminal region (exon 32) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (exon 2-8) and <scene name='User:Jae-Geun_Song/Workbench/plectin/Plakin/1'>plakin domain</scene> (exon 9-30).

-	[[Image:plectin.jpg]]	+	[[Image:plectin.jpg\|left\|300px\|thumb]]

	Schematic domain map of plectin (Winter, 2013)		Schematic domain map of plectin (Winter, 2013)
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	In addition, site-specific missense mutation(R2110W) on plectin rod domain causes an autosomal dominant form of disease termed EBS-Ogna without muscular dystrophy.<ref>PMID: 9067706 </ref>		In addition, site-specific missense mutation(R2110W) on plectin rod domain causes an autosomal dominant form of disease termed EBS-Ogna without muscular dystrophy.<ref>PMID: 9067706 </ref>
	Plectin deficient(-/-) mice also exhibit similar skin and muscle phenotypes of human patients suffering from EBS-MD and died 2-3 days after birth. <ref>PMID: 9389647</ref>		Plectin deficient(-/-) mice also exhibit similar skin and muscle phenotypes of human patients suffering from EBS-MD and died 2-3 days after birth. <ref>PMID: 9389647</ref>
-		+	</StructureSection>
	== References ==		== References ==


	<references/>		<references/>

Alexander Berchansky at 10:43, 8 May 2013

2013-05-08T10:43:01Z

←Older revision		Revision as of 10:43, 8 May 2013
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	== Function and Interactions ==		== Function and Interactions ==
		+	<scene name='Group:MUZIC:Plectin/Plecint/1'>Crystal structure of plectin ABD(magenta) and integrin beta 4 (green) complex</scene> (PDB:[[3f7p]])
	Proteins coordinate various cytoskeletal networks are termed as cytolinkers, which are able to interlink different types of cytoskeletons. Plectin is one of the well-characterized cytolinker and expressed in diverse cell types and tissues, a number of different binding partners of plectin have been identified.		Proteins coordinate various cytoskeletal networks are termed as cytolinkers, which are able to interlink different types of cytoskeletons. Plectin is one of the well-characterized cytolinker and expressed in diverse cell types and tissues, a number of different binding partners of plectin have been identified.

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	The actin binding domain(ABD)in N-terminal globular domain has a role to interact with integrin subunit beta 4 to establish mechanical stability in hemedesmosomes along with its function for binding to actin filament(F-actin). Calmodulin(CaM) is also known to bind the ABD of plectin to modulate the hemidesmosome disassembly <ref> PMID: 19419971 </ref>.		The actin binding domain(ABD)in N-terminal globular domain has a role to interact with integrin subunit beta 4 to establish mechanical stability in hemedesmosomes along with its function for binding to actin filament(F-actin). Calmodulin(CaM) is also known to bind the ABD of plectin to modulate the hemidesmosome disassembly <ref> PMID: 19419971 </ref>.
-
-	<Structure load='3F7P' size='300' frame='true' align='right' caption='Crystal structure of plectin ABD(magenta) and integrin beta 4 (green) complex (PDB:3F7P)' scene='Group:MUZIC:Plectin/Plecint/1' />

	== Pathology ==		== Pathology ==

Alexander Berchansky at 10:40, 8 May 2013

2013-05-08T10:40:01Z

←Older revision		Revision as of 10:40, 8 May 2013
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	'''1. Actin Binding Domain (ABD)'''		'''1. Actin Binding Domain (ABD)'''

-	<~~Structure load='1sh6' size='300' frame='true' align='right' caption='The actin binding domain of plectin (PDB:1SH6)'~~ scene='User:Jae-Geun_Song/Workbench/plectin/Plecin_actin_binding_domain/1'/>	+	<scene name='User:Jae-Geun_Song/Workbench/plectin/Plecin_actin_binding_domain/1'>Plectin</scene> has a canonical actin binding domain in N-terminus, which is consisted of two calponin homology domain(<scene name='User:Jae-Geun_Song/Workbench/plectin/Plecin_actin_binding_domain/3'>CH1 and CH2</scene>)<ref>PMID:9164454</ref>. N-terminal domain of plectin containing ABD interacts with F-actin and regulates actin dynamics in vivo, additionally binding of plectin ABD to vimentin was also reported <ref>PMID: 15128297</ref>.
-		+
-	~~Plectin~~ has a canonical actin binding domain in N-terminus, which is consisted of two calponin homology domain(<scene name='User:Jae-Geun_Song/Workbench/plectin/Plecin_actin_binding_domain/3'>CH1 and CH2</scene>)<ref>PMID:9164454</ref>. N-terminal domain of plectin containing ABD interacts with F-actin and regulates actin dynamics in vivo, additionally binding of plectin ABD to vimentin was also reported <ref>PMID: 15128297</ref>.	+

Alexander Berchansky at 10:37, 8 May 2013

2013-05-08T10:37:53Z

←Older revision		Revision as of 10:37, 8 May 2013
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		+	<StructureSection load='3pe0' size='450' side='right' scene='User:Jae-Geun_Song/Workbench/plectin/Plakin/1' caption=''>
		+
	== Introduction ==		== Introduction ==
	Plectin is a multidomain protein with large size (>500kDa) and versatile binding properties, which abundantly expressed in a wide variety of mammalian tissues and cell types, combined with different binding partners. It has important functions in maintaining the mechanical stability of skin, skeletal muscle and heart.		Plectin is a multidomain protein with large size (>500kDa) and versatile binding properties, which abundantly expressed in a wide variety of mammalian tissues and cell types, combined with different binding partners. It has important functions in maintaining the mechanical stability of skin, skeletal muscle and heart.
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	[[Image:isoforms.gif]]		[[Image:isoforms.gif]]
-
-	<Structure load='3PE0' size='300' frame='true' align='right' caption='Crystal structure of SR4-SR5-SH3 regions in the plakin domain (PDB:3PE0)' scene='User:Jae-Geun_Song/Workbench/plectin/Plakin/1'/>

	== Sequence annotation ==		== Sequence annotation ==
-	The isoform-1 of the human plectin contains 4,684 amino acids [http://www.uniprot.org/uniprot/Q15149 (uniprot:Q15149)]. Plectin can be divided in three main sections; a central coiled-coil rod domain(exon 31), N and C-terminal globular region and exhibits a dumbbell like structure <ref>PMID:8633055</ref>. C-terminal region (exon 32) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (exon 2-8) and plakin domain (exon 9-30).	+	The isoform-1 of the human plectin contains 4,684 amino acids [http://www.uniprot.org/uniprot/Q15149 (uniprot:Q15149)]. Plectin can be divided in three main sections; a central coiled-coil rod domain(exon 31), N and C-terminal globular region and exhibits a dumbbell like structure <ref>PMID:8633055</ref>. C-terminal region (exon 32) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (exon 2-8) and <scene name='User:Jae-Geun_Song/Workbench/plectin/Plakin/1'>plakin domain</scene> (exon 9-30).

	[[Image:plectin.jpg]]		[[Image:plectin.jpg]]

Nikos Pinotsis: /* Sequence annotation */

2013-04-02T11:54:17Z

Sequence annotation

←Older revision		Revision as of 11:54, 2 April 2013
Line 10:		Line 10:

	== Sequence annotation ==		== Sequence annotation ==
-	~~Human~~ plectin contains 4,684 amino acids ~~<ref>PMID~~:~~8633055<~~/~~ref>~~. Plectin can be divided in three main sections; a central coiled-coil rod domain(exon 31), N and C-terminal globular region and exhibits a dumbbell like structure. C-terminal region (exon 32) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (exon 2-8) and plakin domain (exon 9-30).	+	The isoform-1 of the human plectin contains 4,684 amino acids [http://www.uniprot.org/uniprot/Q15149 (uniprot:Q15149)]. Plectin can be divided in three main sections; a central coiled-coil rod domain(exon 31), N and C-terminal globular region and exhibits a dumbbell like structure <ref>PMID:8633055</ref>. C-terminal region (exon 32) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (exon 2-8) and plakin domain (exon 9-30).

	[[Image:plectin.jpg]]		[[Image:plectin.jpg]]

Jae-Geun Song: /* Sequence annotation */

2013-02-28T11:55:20Z

Sequence annotation

←Older revision		Revision as of 11:55, 28 February 2013
Line 10:		Line 10:

	== Sequence annotation ==		== Sequence annotation ==
-	Human plectin contains 4,684 amino acids <ref>PMID:8633055</ref>. Plectin can be divided in three main sections; a central coiled-coil rod domain, N and C-terminal globular region and exhibits a dumbbell like structure. C-terminal region (~~2,828-4,684 aa~~) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (~~180~~-~~396 aa~~) and plakin domain (~~659~~-~~944 aa~~).	+	Human plectin contains 4,684 amino acids <ref>PMID:8633055</ref>. Plectin can be divided in three main sections; a central coiled-coil rod domain(exon 31), N and C-terminal globular region and exhibits a dumbbell like structure. C-terminal region (exon 32) is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin <ref>PMID:3430617</ref>. N-terminal globular region contains actin binding domain comprising two calponin homology (exon 2-8) and plakin domain (exon 9-30).

	[[Image:plectin.jpg]]		[[Image:plectin.jpg]]

Jae-Geun Song: /* Introduction */

2013-02-06T13:33:24Z

Introduction

←Older revision		Revision as of 13:33, 6 February 2013
Line 3:		Line 3:

	The plectin gene has unusual 5'-end diversity, which is alternatively spliced into exon 2 and makes 11 kinds of isoforms.		The plectin gene has unusual 5'-end diversity, which is alternatively spliced into exon 2 and makes 11 kinds of isoforms.
-	Expression level of isofroms is varied in tissues,and some of them are specifically expressed in brain (~~isoforma~~ 1c),skeletal muscle (isoform 1d) and skin(isoform 1a). <ref>PMID:10556294</ref>.	+	Expression level of isofroms is varied in tissues,and some of them are specifically expressed in brain (isoform 1c),skeletal muscle (isoform 1d) and skin(isoform 1a). <ref>PMID:10556294</ref>.

	[[Image:isoforms.gif]]		[[Image:isoforms.gif]]

Jae-Geun Song: /* Introduction */

2013-02-06T13:32:15Z

Introduction

←Older revision		Revision as of 13:32, 6 February 2013
Line 3:		Line 3:

	The plectin gene has unusual 5'-end diversity, which is alternatively spliced into exon 2 and makes 11 kinds of isoforms.		The plectin gene has unusual 5'-end diversity, which is alternatively spliced into exon 2 and makes 11 kinds of isoforms.
-	Expression level of isofroms is varied in tissues,and some of them are specifically expressed in brain,skeletal muscle and skin . <ref>PMID:10556294</ref>.	+	Expression level of isofroms is varied in tissues,and some of them are specifically expressed in brain (isoforma 1c),skeletal muscle (isoform 1d) and skin(isoform 1a). <ref>PMID:10556294</ref>.

	[[Image:isoforms.gif]]		[[Image:isoforms.gif]]