Abstract
The interactions between C99, presenilin, and nicastrin were investigated by a split-ubiquitin assay. We found that C99 homodimerizes and binds weakly to presenilin and strongly to nicastrin. Domain mapping assays revealed the transmembrane and cytoplasmic carboxy-terminal region of C99 is sufficient for the dimerization of C99 and the interaction between C99 and nicastrin. The extracellular domain of C99 is responsible for binding to presenilin. Nicastrin bound to C99 via its transmembrane domain and carboxy-terminal region. These observations suggest that dimerized (or oligomerized) C99 directly interacts with presenilin, and that this interaction is facilitated by nicastrin.
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