NR ATHJ
AU Elvira,G.; Anedda,A.; Juanes,M.E.; Calero,M.; Gasset,M.
TI The subcellular fate of the Prion Protein is determined by a dual translation initiation in the signal peptide coding region
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Cell Biology of PrPc and PrPsc CELL-15
PT Konferenz-Poster
AB Cytoplasmic PrP accounts for a minor subpopulation of the cellular prion protein which is segregated outside the secretory pathway at the co-translational translocation stage. The inadequate translocation efficiency has been ascribed to the properties of its signal peptide sequence and more recently to some leaky ribosome scanning. Using HuPrP and MoPrP signal sequence mutants containing single base insertions causing shift readings at different positions and cell-free translation assays we have found an alternative translation start site at Met8 and Met15. These cell-free translated polypeptide chains, namely MoPrP(Delta1-15) and HuPrP(Delta1-8), account for an about 15 % of the total translation product of the corresponding wt, lack glycosylation and are accessible to externally added proteases. In PrP-null HpL3-4 murine hippocampal neurons HuPrP(Delta1-8) and HuPrP(Delta1-8) are found intracellularly and partition between the cytosolic phase and the membranes of the ER, as judged by co-localization experiments and solubility assays.
AD Gema Elvira, Andrea Anedda, Maria E. Juanes, Maria Gasset, IQFR-CSIC, Spain; Miguel Calero, CNM-ISCIII, Spain
SP englisch
PO Deutschland