Plectin: Difference between revisions
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<Structure load='1sh6' size='400' caption='Mouse plectin actin-binding domain [[1sh6]]' scene= '> | <Structure load='1sh6' size='400' caption='Mouse plectin actin-binding domain [[1sh6]]' scene= '> | ||
== | == Function == | ||
'''Plectin''', a universal and functionally versatile cytolinker protein, 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 <ref>PMID:3430617</ref>. C-terminal region 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:24810881</ref>, <ref>PMID:24940650</ref>. N-terminal globular region contains actin binding domain (ABD) comprising two calponin homology (CH) domains and N-terminal arm, which varies among isoforms. | '''Plectin''', a universal and functionally versatile cytolinker protein, 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 <ref>PMID:3430617</ref>. C-terminal region 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:24810881</ref>, <ref>PMID:24940650</ref>. N-terminal globular region contains actin binding domain (ABD) comprising two calponin homology (CH) domains and N-terminal arm, which varies among isoforms. | ||
Revision as of 11:33, 5 July 2016
<Structure load='1sh6' size='400' caption='Mouse plectin actin-binding domain 1sh6' scene= '>
FunctionFunction
Plectin, a universal and functionally versatile cytolinker protein, 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 [1]. C-terminal region is composed of 6 homologous repeating domains, and this region has a role in binding to intermediate filaments such as vimentin and cytokeratin[2], [3]. N-terminal globular region contains actin binding domain (ABD) comprising two calponin homology (CH) domains and N-terminal arm, which varies among isoforms.
For more details see Group:MUZIC:Plectin.
DiseaseDisease
Mutations in plectin result in skin fragility and blister formation[4].
3D structures of plectin3D structures of plectin
Updated on 05-July-2016
1mb8, 4q59 – hPCN actin-binding domain – human
1sh5, 1sh6 - PCN actin-binding domain – mouse
3pdy, 3pe0 - hPCN plakin domain
2odu, 2odv – hPCN plakin domain (mutant)
4gdo – hPCN rod domain
3f7p, 4q58 - hPCN actin-binding domain + integrin β4 residues 1126-1370
4q57 - hPCN actin-binding domain + calmodulin N terminal
ReferencesReferences
- ↑ Foisner R, Wiche G. Structure and hydrodynamic properties of plectin molecules. J Mol Biol. 1987 Dec 5;198(3):515-31. PMID:3430617
- ↑ Sutoh Yoneyama M, Hatakeyama S, Habuchi T, Inoue T, Nakamura T, Funyu T, Wiche G, Ohyama C, Tsuboi S. Vimentin intermediate filament and plectin provide a scaffold for invadopodia, facilitating cancer cell invasion and extravasation for metastasis. Eur J Cell Biol. 2014 Apr;93(4):157-69. doi: 10.1016/j.ejcb.2014.03.002. Epub, 2014 Apr 15. PMID:24810881 doi:http://dx.doi.org/10.1016/j.ejcb.2014.03.002
- ↑ Bouameur JE, Favre B, Fontao L, Lingasamy P, Begre N, Borradori L. Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure. J Invest Dermatol. 2014 Nov;134(11):2776-83. doi: 10.1038/jid.2014.255. Epub 2014, Jun 18. PMID:24940650 doi:http://dx.doi.org/10.1038/jid.2014.255
- ↑ Pfendner E, Rouan F, Uitto J. Progress in epidermolysis bullosa: the phenotypic spectrum of plectin mutations. Exp Dermatol. 2005 Apr;14(4):241-9. PMID:15810881 doi:http://dx.doi.org/10.1111/j.0906-6705.2005.00324.x