Function
Plectin, a universal and functionally versatile cytolinker protein, can be divided in three main sections; a central coiled-coil rod domain (residues 1492-1530), N and C-terminal globular region and exhibits a dumbbell like structure [1]. C-terminal region is composed of 6 homologous repeating domains (repeat#6 contains residues 4403-4606), 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) (residues 175-400) comprising of two calponin homology (CH) domains, plakin domain (residues 300-1372) and N-terminal arm, which varies among isoforms.
For more details see Group:MUZIC:Plectin.
Disease
Mutations in plectin result in skin fragility and blister formation[4].
- ↑ 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:https://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:https://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:https://dx.doi.org/10.1111/j.0906-6705.2005.00324.x
