COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform

@article{citeulike:1891604, abstract = {Efficient formation of scrapie isoform of prion protein (PrPSc) requires targeting PrPSc by glycophosphatidyl inositol (GPI) anchors to caveolae-like domains (CLDs). Redirecting the cellular isoform of prion protein (PrPC) to clathrin-coated pits by creating chimeric PrP molecules with four different COOH-terminal transmembrane domains prevented the formation of PrPSc. To determine if these COOH-terminal transmembrane segments prevented PrPC from refolding into PrPSc by altering the structure of the polypeptide, we fused the 28-aa COOH termini from the Qa protein. Two COOH-terminal Qa segments differing by a single residue direct the transmembrane protein to clathrin-coated pits or the GPI form to CLDs; PrPSc was formed from GPI-anchored PrPC but not from transmembrane PrPC. Our findings argue that PrPSc formation is restricted to a specific subcellular compartment and as such, it is likely to involve auxiliary macromolecules found within CLDs. 10.1073/pnas.94.6.2333}, author = {Kaneko, Kiyotoshi and Vey, Martin and Scott, Michael and Pilkuhn, Susanne and Cohen, Fred E. and Prusiner, Stanley B. }, citeulike-article-id = {1891604}, doi = {10.1073/pnas.94.6.2333}, journal = {Proceedings of the National Academy of Sciences}, keywords = {prp, traffic}, month = {March}, number = {6}, pages = {2333--2338}, posted-at = {2007-11-09 23:32:08}, priority = {2}, title = {COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform}, url = {http://dx.doi.org/10.1073/pnas.94.6.2333}, volume = {94}, year = {1997} }

TY - JOUR ID - citeulike:1891604 L3 - citeulike-article-id:1891604 TI - COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform JF - Proceedings of the National Academy of Sciences VL - 94 IS - 6 SP - 2333 EP - 2338 N2 - Efficient formation of scrapie isoform of prion protein (PrPSc) requires targeting PrPSc by glycophosphatidyl inositol (GPI) anchors to caveolae-like domains (CLDs). Redirecting the cellular isoform of prion protein (PrPC) to clathrin-coated pits by creating chimeric PrP molecules with four different COOH-terminal transmembrane domains prevented the formation of PrPSc. To determine if these COOH-terminal transmembrane segments prevented PrPC from refolding into PrPSc by altering the structure of the polypeptide, we fused the 28-aa COOH termini from the Qa protein. Two COOH-terminal Qa segments differing by a single residue direct the transmembrane protein to clathrin-coated pits or the GPI form to CLDs; PrPSc was formed from GPI-anchored PrPC but not from transmembrane PrPC. Our findings argue that PrPSc formation is restricted to a specific subcellular compartment and as such, it is likely to involve auxiliary macromolecules found within CLDs. 10.1073/pnas.94.6.2333 KW - prp KW - traffic AU - Kaneko, Kiyotoshi AU - Vey, Martin AU - Scott, Michael AU - Pilkuhn, Susanne AU - Cohen, Fred AU - Prusiner, Stanley PY - 1997/03/18/ UR - http://dx.doi.org/10.1073/pnas.94.6.2333 ER -