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Phosphorylation of the human CTF resulted in a shift in electrophoretic mobility from a single major species of 18 kDa to a doublet of 20\u201323 kDa. This mobility shift was also observed with human PS1 that had been transfected into mouse neuroblastoma (N2a) cells. Treatment of the phosphorylated CTF doublet with phage \u03bb protein phosphatase eliminated the 20- to 23-kDa doublet while enhancing the 18-kDa species, consistent with the interpretation that the electrophoretic mobility shift was due to the addition of phosphate to the 18-kDa species. The NTF and CTF eluted from a gel filtration column at an estimated mass of over 100 kDa, suggesting that these fragments exist as an oligomerized species. Upon phosphorylation of the PS1 CTF, the apparent mass of the NTF- or CTF-containing oligomers was unchanged. Thus, the association of PS1 fragments may be maintained during cycles of phosphorylation\/dephosphorylation of the PS1 CTF.<\/jats:p>","DOI":"10.1073\/pnas.94.10.5090","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:31:39Z","timestamp":1027679499000},"page":"5090-5094","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":128,"title":["Evidence for phosphorylation and oligomeric assembly of presenilin\u20091"],"prefix":"10.1073","volume":"94","author":[{"given":"Mary","family":"Seeger","sequence":"first","affiliation":[{"name":"Laboratory of Alzheimer Research, Department of Neurology and Neuroscience, Cornell University Medical College, New York, NY 10021; Laboratory of Molecular and Cellular Neuroscience and Fisher Center for Research on Alzheimer Disease, The Rockefeller University, New York, NY 10021; Laboratory of Biochemistry and Molecular Pharmacology, Section of Experimental Alcohol and Drug Addiction Research, Department of Clinical Neuroscience, Karolinska Institute, S-171 77 Stockholm, Sweden; 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