Presenilin 1 is actively degraded by the 26S proteasome

Neurobiology of Aging

Volumn 19, Issue SUPPL. 1, 1998, Pages

  Fraser, P E ^a   Levesque, G ^a   Yu, G ^a   Mills, L R ^b   Thirlwell, J ^b   Frantseva, M ^b   Gandy, S E ^c   Seeger, M ^d   Carlen, P L ^b   St George Hyslop, P ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b TORONTO WESTERN HOSPITAL   (Canada)

^c NEW YORK UNIVERSITY   (United States)

^d ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Alzheimer Disease; Degradation; Endoplasmic reticulum; Presenilin; Proteasome; Proteolysis; PS1; PS2; Transmembrane protein

Indexed keywords

CYTOPLASM PROTEIN; MEMBRANE PROTEIN; PRESENILIN 1; PRESENILIN 2; PROTEASOME;

ALZHEIMER DISEASE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; BRAIN; CONFERENCE PAPER; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GENE MUTATION; IMMUNOPRECIPITATION; METABOLISM; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT;

ALZHEIMER DISEASE; ANIMALS; BLOTTING, WESTERN; CACO-2 CELLS; HIPPOCAMPUS; HUMANS; MEMBRANE PROTEINS; MICE; NF-KAPPA B; PEPTIDE HYDROLASES; PRESENILIN-1; PROTEASOME ENDOPEPTIDASE COMPLEX; RATS; RATS, WISTAR;

EID: 0031968723     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-4580(98)00029-3     Document Type: Conference Paper

References (18)

1. Biederer T., Volkwein C., Sommer T. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15:1996;2069-2076.
2. Citron M., Westaway D., Xia W., Carlson G., Diehl T. S., Levesque G., Johnson-Wood K., Lee M., Seubert P., Davis A., Schenk D., St George-Hyslop P., Selkoe D. J. Mutant presenilins of Alzheimer's Disease increase production of 42 residue amyloid B-protein in both transfected cells and transgenic mice. Nature Med. 3:1997;67-72.
3. Coux O., Tanaka K., Goldberg A. L. Structure and functions of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65:1996;801-847.
4. De Strooper B., Beullens M., Contreras B., Craessaerts K., Moechars D., Bollen M., Fraser P., St George-Hyslop P., Van Leuven F. Postranslational modification, subcellular localization and membrane orientation of the Alzheimer's Disease associated Presenilins. J. Biol. Chem. 272:1997;3590-3598.
5. Fenteany G., Standaert R. F., Lane W. S., Choi S., Corey E. J., Schreiber S. L. Inhibition of proteasome activities and subunit-specific amino terminal threonine modification by lactacystin. Science. 268:1995;726-731.
6. Hiller M. M., Finger A., Schweiger M., Wolf D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science. 273:1996;1725-1728.
7. Jensen T. J., Loo M. A., Pind S., Williams D. B., Goldberg A. L., Riordan J. R. Multiple proteolytic systems including the proteasome contribute to CFTR processing. Cell. 83:1995;129-135.
8. Levy-Lahad E., Wijsman E. M., Nemens E., Anderson L., Goddard K. A., Weber J. L., Bird T. D., Schellenberg G. D. A familial Alzheimer's Disease locus on chromosome 1. Science. 269:1995;970-973.
9. Plemper R. K., Bohmler S., Bordallo J., Sommer T., Wolf D. H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 388:1997;891-891.
10. Podlisny M. B., Ostaszewski B. L., Squazzo S. L., Koo E. H., Rydell R. E., Teplow D. B., Selkoe D. J. Aggregation of secreted amyloid beta protein into SDS-stable oligomers in cell culture. J. Biol. Chem. 270:1995;9564-9570.
11. Rock K. L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A. L. Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771.
12. Rogaev E. I., Sherrington R., Rogaeva E. A., Levesque G., Ikeda M., Liang Y., Chi H., Lin C., Holman K., Tsuda T. Familial Alzheimer's disease in kindreds with missense mutations in a novel gene on chromosome 1 related to the Alzheimer's Disease type 3 gene. Nature. 376:1995;775-778.
13. Sherrington R., Rogaev E. I., Liang Y., Rogaeva E., Levesque G., Ikeda M., Chi H., Lin C., Holman K., Tsuda T. Cloning of a gene bearing missense mutations in early onset familial Alzheimer's disease. Nature. 375:1995;754-760.
14. Stoppini L., Buchs P. A., Muller D. Lesion induced neurite sprouting and synapse formation in hippocampal organotypic cultures. Neuroscience. 57:1993;985-994.
15. Thinakaran G., Borchelt D. R., Lee M. K., Slunt H. H., Spitzer L., Kim G., Ratovisky T., Davenport F., Nordstedt C., Seeger M. Endoproteolysis of Presenilin 1 and accumulation of processed derivatives in vivo. Neuron. 17:1996;181-190.
16. Walter J., Capell A., Grunberg J., Pesold B., Schindzielorz A., Prior R., Podlisny M. B., Fraser P., St George-Hyslop P., Selkoe D. The Alzheimer's disease associated Presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol. Med. 2:1996;673-691.
17. Wiertz E. J., Jones T. R., Sun L., Bogyo M., Geuze H. J., Ploegh H. L. The human cytomegalovirus US11 gene product dislocates MHC class 1 heavy chains from the endoplasmic reticulum to the cytosol. Cell. 84:1997;769-779.
18. Yuk M. H., Lodish H. F. Two pathways for the degradation of the H2 subunit of the asialoglycoprotein receptor in the endoplasmic reticulum. J. Cell. Biol. 123:1993;1735-1749.