Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871353 | FEBS Letters | 2013 | 10 Pages |
Abstract
Gene duplication provides genetic material required for functional diversification. An interesting example is the amyloid precursor protein (APP) protein family. The APP gene family has experienced both expansion and contraction during evolution. The three mammalian members have been studied quite extensively in combined knock out models. The underlying assumption is that APP, amyloid precursor like protein 1 and 2 (APLP1, APLP2) are functionally redundant. This assumption is primarily supported by the similarities in biochemical processing of APP and APLPs and on the fact that the different APP genes appear to genetically interact at the level of the phenotype in combined knockout mice. However, unique features in each member of the APP family possibly contribute to specification of their function. In the current review, we discuss the evolution and the biology of the APP protein family with special attention to the distinct properties of each homologue. We propose that the functions of APP, APLP1 and APLP2 have diverged after duplication to contribute distinctly to different neuronal events. Our analysis reveals that APLP2 is significantly diverged from APP and APLP1.
Keywords
FOSSVZWNT5AMAP2Dab1DKOApoER2APPFBJ murine osteosarcoma viral oncogene homologwingless-type MMTV integration site family, member 5APCPAPLPGFAPVLDLRlong term potentiationLTPcortical plateDisabled-1EvolutionCortexArcventricular zonesubventricular zonedouble knockoutknockoutFunctional divergenceGlial fibrillary acidic proteinmicrotubule-associated protein 2amyloid precursor proteincalcium/calmodulin-dependent serine protein kinaseCASKApolipoprotein E receptor 2Very low density lipoprotein receptor
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Authors
S. Ali M. Shariati, Bart De Strooper,