Regulation of focal adhesion formation and filopodia extension by the cellular prion protein (PrPC).
While the prion protein (PrP) is clearly involved in neuropathology, its physiological roles remain elusive. Here, we demonstrate PrP functions in cell-substrate interaction in Drosophila S2, N2a and HeLa cells. PrP promotes cell spreading and/or filopodia formation when overexpressed, and lamellipodia when downregulated. Moreover, PrP normally accumulates in focal adhesions (FAs), and its downregulation leads to reduced FA numbers, increased FA length, along with Src and focal adhesion kinase (FAK) activation. Furthermore, its overexpression elicits the formation of novel FA-like structures, which require intact reggie/flotillin microdomains. Altogether, PrP modulates process formation and FA dynamics, possibly via signal transduction involving FAK and Src.
Schrock
Yvonne
Y
Department of Biology, University of Konstanz, Universitaetsstrasse 10, 78464 Konstanz, Germany.
Solis
Gonzalo P
GP
Stuermer
Claudia A O
CA
D000818:Animals; D022001:Focal Adhesions / Q000502:physiology*; D006367:HeLa Cells; D006801:Humans; D051379:Mice; D018621:PrPC Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D011554:Pseudopodia / Q000502:physiology*; D034741:RNA, Small Interfering / Q000235:genetics; D051381:Rats
D018621:PrPC Proteins; D034741:RNA, Small Interfering