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K16 is a further new candidate for homotypic intermediate filament protein interactions
Author(s) -
Trost Andrea,
Costa Ivano,
Jakab Martin,
Ritter Markus,
Haim Martina,
Hintner Helmut,
Bauer Johann W.,
Önder Kamil
Publication year - 2010
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/j.1600-0625.2010.01071.x
Subject(s) - keratin , intermediate filament , hacat , microbiology and biotechnology , keratin 6a , chemistry , keratin 8 , biology , keratin 5 , cytoskeleton , in vitro , cell , biochemistry , genetics
Please cite this paper as: K16 is a further new candidate for homotypic intermediate filament protein interactions. Experimental Dermatology 2010; 19 : e241–e250. Abstract: Keratin filaments form obligatory heterodimers consisting of one type I and one type II keratin that build the intermediate filaments (IF). These filaments mediate resilience and mechanical strength to epithelial cells and maintain tissue integrity. Specific type I/type II pairs are co‐expressed in vivo and serve as markers for distinct tissue layers and cell differentiation states. Heterodimerization has been regarded the undisrupted hallmark of IF. We show now that recombinantly expressed cytokeratin 16 (K16) interacts with itself and forms homodimers even in denaturating SDS–PAGE analysis. Detailed FRET experiments in HaCaT keratinocytes were in accordance with our in vitro observations and showed clearly that K16 is able to form strong homodimers. Homotypic keratin interactions has been previously shown for keratin 17 (K17) and keratin 18 (K18) by Schnabel et al. ( Biochim Biophys Acta , 1998: 1403: 158), and we now proved K16 to be the third type I keratin that is able to form homodimers.