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Molecular and Cellular Biology, January 2006, p. 559-568, Vol. 26, No. 2
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.2.559-568.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Epiplakin Is Dispensable for Skin Barrier Function and for Integrity of Keratin Network Cytoarchitecture in Simple and Stratified Epithelia

Daniel Spazierer,1,{dagger} Peter Fuchs,1,{dagger} Siegfried Reipert,1 Irmgard Fischer,1 Matthias Schmuth,2 Hans Lassmann,3 and Gerhard Wiche1*

Department of Molecular Cell Biology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria,1 Department of Dermatology and Venereology, Medical University of Innsbruck, 6020 Innsbruck, Austria,2 Center for Brain Research, Medical University of Vienna, 1090 Vienna, Austria3

Received 21 July 2005/ Returned for modification 23 August 2005/ Accepted 19 October 2005

Epiplakin, a giant epithelial protein of >700 kDa, belongs to the plakin family of cytolinker proteins. It represents an atypical family member, however, as it consists entirely of plakin repeat domains but lacks any of the other domains commonly shared by plakins. Hence, its putative function as a cytolinker protein remains to be shown. To investigate epiplakin's biological role, we generated epiplakin-deficient mice by gene targeting in embryonic stem cells. Epiplakin-deficient mice were viable and fertile, without developing any discernible phenotype. Ultrastructurally, their epidermis revealed no differences compared to wild-type littermates, and cornified envelopes isolated from skin showed no alterations in shape or stability. Furthermore, neither embryonal formation nor later function of the epithelial barrier was affected. In primary cultures of epiplakin-deficient keratinocytes, the organization of actin filaments, microtubules, and keratin networks was found to be normal. Similarly, no alterations in keratin network organization were observed in simple epithelia of small intestine and liver or in primary hepatocytes. We conclude that, despite epiplakin's abundant and highly specific expression in stratified and simple epithelia, its absence in mice does not lead to severe skin dysfunctions, nor has it detectable consequences for keratin filament organization and cytoarchitecture of cells.

* Corresponding author. Mailing address: Department of Molecular Cell Biology, University of Vienna, Dr. Bohrgasse 9, A-1030 Vienna, Austria. Phone: 43 1 4277 52852. Fax: 43 1 4277 52854. E-mail: gerhard.wiche{at}univie.ac.at.

{dagger} D.S. and P.F. contributed equally to this work.

Molecular and Cellular Biology, January 2006, p. 559-568, Vol. 26, No. 2
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.2.559-568.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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  • Spazierer, D., Raberger, J., Gross, K., Fuchs, P., Wiche, G. (2008). Stress-induced recruitment of epiplakin to keratin networks increases their resistance to hyperphosphorylation-induced disruption. J. Cell Sci. 121: 825-833 [Abstract] [Full Text]  
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