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

ABSTRACT: 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 PKCdelta were significantly elevated, and increased migration rates, as assesse

SUBMITTER: Osmanagic-Myers S 

PROVIDER: S-EPMC2064261 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature