NR AUYB
AU Beck,K.E.; Kay,J.G.; Braun,J.E.
TI Rdj2, a J protein family member, interacts with cellular prion PrPc
QU Biochemical and Biophysical Research Communications 2006 Aug 4; 346(3): 866-71
PT journal article
AB PrPc is a glycosylphosphatidylinositol (GPI) anchored glycoprotein of unknown function. Misfolding of normal cellular PrPc to the pathogenic PrPsc is the hallmark of prion diseases (transmissible spongiform encephalopathies). Prion diseases are characterized by extensive neurodegeneration and early death. Understanding how PrPc maintains its correct conformation is a major endeavor of current inquiry. Here we demonstrate a novel interaction between PrPc and the J protein family member, Rdj2 (DjA2; Dj3, Dnj3, Cpr3, and Hirip4). The importance of the J protein family in the cellular folding machinery has been recognized for many years. The PrPc/Rdj2 association was direct and concentration-dependent. Other J proteins such as CSPalpha and auxilin did not associate with PrPc in the absence of ATP, demonstrating the specificity of the PrPc/J protein interaction. These findings suggest that the J protein family serves as a 'folding catalyst' for PrPc and implicates Rdj2 as a factor in the protection against prion diseases.
MH Adenosine Triphosphate/pharmacology; Animals; HSP40 Heat-Shock Proteins/*classification/genetics/*metabolism; PrPc Proteins/*metabolism; Protein Binding; Rats; Research Support, Non-U.S. Gov't; Temperature
AD Hotchkiss Brain Institute, Department of Physiology and Biophysics, University of Calgary, Calgary, Alta., Canada T2N 4N1.
SP englisch
PO USA