Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment

Joseph D. Buxbaum, Eun Kyoung Choi, Yuxia Luo, Christina Lilliehook, Annette C. Crowley, David E. Merriam, Wilma Wasco

Research output: Contribution to journalArticlepeer-review

301 Scopus citations

Abstract

Most early-onset familial Alzheimer disease (AD) cases are caused by mutations in the highly related genes presenilin 1 (PS1) and presenilin 2 (PS2). Presenilin mutations produce increases in β-amyloid (Aβ) formation and apoptosis in many experimental systems. A cDNA (ALG-3) encoding the last 103 amino acids of PS2 has been identified as a potent inhibitor of apoptosis. Using this PS2 domain in the yeast two-hybrid system, we have identified a neuronal protein that binds calcium and presenilin, which we call calsenilin. Calsenilin interacts with both PS1 and PS2 in cultured cells, and can regulate the levels of a proteolytic product of PS2. Thus, calsenilin may mediate the effects of wild-type and mutant presenilins on apoptosis and on Aβ formation. Further characterization of calsenilin may lead to an understanding of the normal role of the presenilins and of the role of the presenilins in Alzheimer disease.

Original languageEnglish
Pages (from-to)1177-1181
Number of pages5
JournalNature Medicine
Volume4
Issue number10
DOIs
StatePublished - Oct 1998

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