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TMP21 is a ubiquitously expressed protein that is involved in vesicular targeting and protein transport. More recent experiments have shown that it is also a component in the presenilin complex and modulates the gamma-secretase, but not the epsilon-secretase cleavage activity of the amyloid precursor protein. The presenilin complex is composed of the proteins APH1, nicastrin, and PEN2 in addition to presenilin-1. Together, these proteins cleave the amyloid precursor protein at what is known as the gamma- and epsilon-sites, and can lead to the accumulation of the Abeta cleavage product that is associated with Alzheimer's disease. Co-immunoprecipitation experiments using antibodies against these proteins also yielded TMP21, indicating that TMP21 may play a role in the regulation of this complex. Suppression of TMP21 expression by siRNA in transfected cells caused increased gamma-secretase activity and Abeta production, but not epsilon-secretase activity, demonstrating that TMP21 can modulate gamma-secretase activity.
