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Published 14 August 2006. doi:10.1083/jcb.200605172
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 4, 557-568
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Article

Plectin-controlled keratin cytoarchitecture affects MAP kinases involved in cellular stress response and migration



Selma Osmanagic-Myers, Martin Gregor, Gernot Walko, Gerald Burgstaller, Siegfried Reipert, and Gerhard Wiche

Department of Molecular Cell Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria

Correspondence to Gerhard Wiche: gerhard.wiche{at}univie.ac.at

Plectin is a major intermediate filament (IF)–based cytolinker protein that stabilizes cells and tissues mechanically, regulates actin filament dynamics, and serves as a scaffolding platform for signaling molecules. In this study, we show that plectin deficiency is a cause of aberrant keratin cytoskeleton organization caused by a lack of orthogonal IF cross-linking. Keratin networks in plectin-deficient cells were more susceptible to osmotic shock–induced retraction from peripheral areas, and their okadaic acid–induced disruption (paralleled by stress-activated MAP kinase p38 activation) proceeded faster. Basal activities of the MAP kinase Erk1/2 and of the membrane-associated upstream protein kinases c-Src and PKC{delta} were significantly elevated, and increased migration rates, as assessed by in vitro wound-closure assays and time-lapse microscopy, were observed. Forced expression of RACK1, which is the plectin-binding receptor protein for activated PKC{delta}, in wild-type keratinocytes elevated their migration potential close to that of plectin-null cells. These data establish a link between cytolinker-controlled cytoarchitecture/scaffolding functions of keratin IFs and specific MAP kinase cascades mediating distinct cellular responses.

S. Osmanagic-Myers, M. Gregor, and G. Walko contributed equally to this paper.

Abbreviations used in this paper: EBS, epidermolysis bullosa simplex; HD, hemidesmosome; IF, intermediate filament; OA, okadaic acid; RACK, receptor for activated C kinase; SB, Sorensen's buffer.


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