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FE65 is an adaptor protein that consists of three protein-protein interaction domains. The most
C-terminal domain, PID2, binds to the cytoplasmic tail of the beta-amyloid precursor protein (bPP),
rning/memory phenotype, Ms. Cool has been working on a microarray experiment comparing gene
expression profiles from cerebral cortex of five knockout mice and their wildtype control
littermates. Ms. Cool currently analyzing the gene data and planning quantitative real-time PCR
experiments to confirm the small fold-changes revealed through the array. In order to further
characterize the P60 isoform, Ms. Cool has also done immunofluorescence to compare the
intracellular localizations of P97 and P60 using knockout and wildtype primary neuron cultures.
FE65’s nuclear localization has been confirmed, and preliminary evidence suggests P60 is also found
in the nucleus. Cloning of FE65 to determine P60’s likely translation start site has also been
accomplished. Ms. Cool’s next step is to use this clone in a functional study to test P60’s ability
to influence transcription.
Publication resulting from support:
1. Wang B, Hu Q, Hearn MG, Shimizu K, Ware CB, Liggit DH, Cool BH, Storm DR, Martin GM. Isoform
specific knockout of FE65 leads to impaired learning and memory. Journal of Neuroscience Research.
75(1): 12-24, 2004
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